35737-15-6 | - Page 8 of 10 - Indole Building Blocks

Hermant, Yann team published research on Journal of Natural Products in 2021 | 35737-15-6

35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., Synthetic Route of 35737-15-6

Previous studies have identified that indole-oxidases are present in P. putida, whose major ligands are heterocyclic substrates and have an interesting affinity when the substrate is indole. 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. These enzymes oxidize the ring so the substrate turns into Indigo. Synthetic Route of 35737-15-6.

Hermant, Yann;Palpal-latoc, Dennise;Kovalenko, Nadiia;Cameron, Alan J.;Brimble, Margaret A.;Harris, Paul W. R. research published 《 The total chemical synthesis and biological evaluation of the cationic antimicrobial peptides, laterocidine and brevicidine》, the research content is summarized as follows. Antimicrobial resistance is a significant threat to public health systems worldwide, prompting immediate attention to develop new therapeutic agents with novel mechanisms of action. Recently, two new cationic non-ribosomal peptides (CNRPs), laterocidine and brevicidine, were discovered from Brevibacillus laterosporus through a global genome-mining approach. Both laterocidine and brevicidine exhibit potent antimicrobial activity toward Gram-neg. bacteria, including difficult-to-treat Pseudomonas aeruginosa and colistin-resistant Escherichia coli, and a low risk of resistance development. Herein, we report the first total syntheses of laterocidine and brevicidine via an efficient and high-yielding combination of solid-phase synthesis and solution-phase macrolactamization. The crucial depsipeptide bond of the macrolactone rings of laterocidine and brevicidine was established on-resin between the side-chain hydroxy group of Thr⁹ with Alloc-Gly-OH or Alloc-Ser(tBu)-OH, resp. A conserved glycine residue within the lactone macrocycle is exploited for the initial immobilization onto the hyper acid-labile 2-chlorotrityl chloride resin, subsequently enabling an efficient solution-phase macrocyclization to yield laterocidine and brevicidine in 36% and 10% overall yields, resp. (with respect to resin loading). A biol. evaluation against both Gram-pos. and Gram-neg. bacteria demonstrated that synthetic laterocidine and brevicidine possessed a potent and selective antimicrobial activity toward Gram-neg. bacteria, in accordance with the isolated compounds

Referemce:
Indole alkaloid derivatives as building blocks of natural products from Bacillus thuringiensis and Bacillus velezensis and their antibacterial and antifungal activity study,
Preparation of Indole Containing Building Blocks for the Regiospecific Construction of Indole Appended Pyrazoles and Pyrroles

Hojo, Hironobu team published research on Angewandte Chemie, International Edition in 2021 | 35737-15-6

Indole, first isolated in 1866, has the molecular formula C8H7N, and it is commonly synthesized from phenylhydrazine and pyruvic acid, 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. although several other procedures have been discovered.Indole is a colourless solid having a pleasant fragrance in highly dilute solutions. It melts at 52.5° C (126.5° F). Synthetic Route of 35737-15-6.

Hojo, Hironobu;Takei, Toshiki;Asahina, Yuya;Okumura, Nobuaki;Takao, Toshifumi;So, Masatomo;Suetake, Isao;Sato, Takeshi;Kawamoto, Akihiro;Hirabayashi, Yoshio research published 《 Total synthesis and structural characterization of Caveolin-1》, the research content is summarized as follows. Caveolin-1, which is an essential protein for caveola formation, was chem. synthesized. It is composed of 177 amino acid residues, is triply palmitoylated at the C-terminal region, and is inserted into the lipid bilayer to form a V-shaped structure in the middle of the polypeptide chain. The entire sequence was divided into five peptide segments, each of which was synthesized by the solid-phase method. To improve the solubility of the C-terminal region, O-acyl isopeptide structures were incorporated. After ligation by the thioester method and the introduction of the palmitoyl groups, all the protecting groups were removed and the isopeptide structures were converted into the native peptide bond. Finally, the obtained polypeptide was successfully inserted into bicelles, thus showing the success of the synthesis.

Hostetler, Matthew A. team published research on ACS Chemical Biology in 2021 | 35737-15-6

COA of Formula: C26H22N2O4, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Hostetler, Matthew A.;Smith, Chloe;Nelson, Samantha;Budimir, Zachary;Modi, Ramya;Woolsey, Ian;Frerk, Autumn;Baker, Braden;Gantt, Jessica;Parkinson, Elizabeth I. research published 《 Synthetic natural product inspired cyclic peptides》, the research content is summarized as follows. Natural products are a bountiful source of bioactive mols. Unfortunately, discovery of novel bioactive natural products is challenging due to cryptic biosynthetic gene clusters, low titers, and arduous purifications. Herein, we describe SNaPP (Synthetic Natural Product Inspired Cyclic Peptides), a method for identifying NP-inspired bioactive peptides. SNaPP expedites bioactive mol. discovery by combining bioinformatics predictions of nonribosomal peptide synthetases with chem. synthesis of the predicted natural products (pNPs). SNaPP utilizes a recently discovered cyclase, the penicillin binding protein-like cyclase, as the lynchpin for the development of a library of head-to-tail cyclic peptide pNPs. Anal. of 500 biosynthetic gene clusters allowed for identification of 131 novel pNPs. Fifty-one diverse pNPs were synthesized using solid phase peptide synthesis and solution-phase cyclization. Antibacterial testing revealed 14 pNPs with antibiotic activity, including activity against multidrug-resistant Gram-neg. bacteria. Overall, SNaPP demonstrates the power of combining bioinformatics predictions with chem. synthesis to accelerate the discovery of bioactive mols.

Huhmann, Susanne team published research on ChemBioChem in 2021 | 35737-15-6

Synthetic Route of 35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

In addition to indoleacetic acid, indigo, and tryptophan, numerous compounds obtainable from plant or animal sources contain the indole molecular structure. 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. The best-known group of these compounds is the indole alkaloids, members of which have been isolated from plants representing more than 30 families. Synthetic Route of 35737-15-6.

Huhmann, Susanne;Nyakatura, Elisabeth K.;Rohrhofer, Anette;Moschner, Johann;Schmidt, Barbara;Eichler, Jutta;Roth, Christian;Koksch, Beate research published 《 Systematic Evaluation of Fluorination as Modification for Peptide-Based Fusion Inhibitors against HIV-1 Infection》, the research content is summarized as follows. With the emergence of novel viruses, the development of new antivirals is more urgent than ever. A key step in human immunodeficiency virus type 1 (HIV-1) infection is six-helix bundle formation within the envelope protein subunit gp41. Selective disruption of bundle formation by peptides has been shown to be effective; however, these drugs, exemplified by T20, are prone to rapid clearance from the patient. The incorporation of non-natural amino acids is known to improve these pharmacokinetic properties. Here, we evaluate a peptide inhibitor in which a critical Ile residue is replaced by fluorinated analogs. We characterized the influence of the fluorinated analogs on the biophys. properties of the peptide. Furthermore, we show that the fluorinated peptides can block HIV-1 infection of target cells at nanomolar levels. These findings demonstrate that fluorinated amino acids are appropriate tools for the development of novel peptide therapeutics.

Islam, Yamir team published research on Journal of Pharmaceutical Sciences (Philadelphia, PA, United States) in 2021 | 35737-15-6

Application of C26H22N2O4, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Islam, Yamir;Ehtezazi, Parinaz;Cashmore, Andrew;Marinsalda, Elena;Leach, Andrew G.;Coxon, Christopher R.;Fatokun, Amos A.;Sexton, Darren W.;Khan, Iftikhar;Zouganelis, Georgios;Downing, James;Pluchino, Stefano;Sivakumaran, Muttuswamy;Teixido, Meritxell;Ehtezazi, Touraj research published 《 The inclusion of a matrix metalloproteinase-9 responsive sequence in self-assembled peptide-based brain-targeting nanoparticles improves the efficiency of nanoparticles crossing the blood-brain barrier at elevated MMP-9 levels》, the research content is summarized as follows. This study investigated whether the inclusion of a matrix metalloproteinase-9 (MMP-9) responsive sequence in self-assembled peptide-based brain-targeting nanoparticles (NPs) would enhance the blood-brain barrier (BBB) penetration when MMP-9 levels are elevated both in the brain and blood circulation. Brain-targeting peptides were conjugated at the N-terminus to MMP-9-responsive peptides, and these were conjugated at the N-terminus to lipid moiety (cholesteryl chloroformate or palmitic acid). Two constructs did not have MMP-9-responsive peptides. NPs were characterized for size, charge, critical micelle concentration, toxicity, blood compatibility, neural cell uptake, release profiles, and in vitro BBB permeability simulating normal or elevated MMP-9 levels. The inclusion of MMP-9-sensitive sequences did not improve the release of a model drug in the presence of active MMP-9 from NPs compared to distilled water. ¹⁹F NMR studies suggested the burial of MMP-9-sensitive sequences inside the NPs making them inaccessible to MMP-9. Only cholesterol-GGGCKAPETALC (responsive to MMP-9) NPs showed <5% hemolysis, <1 pg/mL release of IL-1β at 500μg/mL from THP1 cells, with 70.75 ± 5.78% of NPs crossing the BBB at 24 h in presence of active MMP-9. In conclusion, brain-targeting NPs showed higher transport across the BBB model when MMP-9 levels were elevated and the brain-targeting ligand was responsive to MMP-9.

Jacobsson, Erik team published research on Journal of Natural Products in 2021 | 35737-15-6

Jacobsson, Erik;Peigneur, Steve;Andersson, Haakan S.;Laborde, Quentin;Strand, Malin;Tytgat, Jan;Goeransson, Ulf research published 《 Functional Characterization of the Nemertide α Family of Peptide Toxins》, the research content is summarized as follows. Peptide toxins find use in medicine, biotechnol., and agriculture. They are exploited as pharmaceutical tools, particularly for the investigation of ion channels. Here, we report the synthesis and activity of a novel family of peptide toxins: the cystine-knotted α nemertides. Following the prototypic α-1 and -2 (1 and 2), six more nemertides were discovered by mining of available nemertean transcriptomes. Here, we describe their synthesis using solid phase peptide chem. and their oxidative folding by using an improved protocol. Nemertides α-2 to α-7 (2-7) were produced to characterize their effect on voltage-gated sodium channels (Blatella germanica BgNa_V1 and mammalian Na_Vs1.1-1.8). In addition, ion channel activities were matched to in vivo tests using an Artemia microwell assay. Although nemertides demonstrate high sequence similarity, they display variability in activity on the tested Na_Vs. The nemertides are all highly toxic to Artemia, with EC₅₀ values in the sub-low micromolar range, and all manifest preference for the insect BgNa_V1 channel. Structure-activity relationship anal. revealed key residues for Na_V-subtype selectivity. Combined with low EC₅₀ values (e.g., Na_V1.1: 7.9 nM (α-6); Na_V1.3: 9.4 nM (α-5); Na_V1.4: 14.6 nM (α-4)) this underscores the potential utility of α-nemertides for rational optimization to improve selectivity.

Joshi, Vinay G. team published research on Applied Microbiology and Biotechnology in 2021 | 35737-15-6

Electric Literature of 35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Joshi, Vinay G.;Chindera, Kantaraja;Bais, Manish V.;Sajjanar, Basavaraj;Tiwari, Ashok K.;Kumar, Satish research published 《 Novel peptide (RATH) mediated delivery of peptide nucleic acids for antiviral interventions》, the research content is summarized as follows. The peptide nucleic acid (PNA) is a chimeric mol. with the nucleobases connected by peptide bonds. This chimeric nature gives the PNA certain therapeutic advantages over natural antisense nucleic acid mols. The PNA probes are known for its better and stronger complementation with target nucleic acids. However, cellular delivery of PNA is a major hurdle due to the charge-neutral nature of the PNA. For cellular delivery of PNA, peptide-PNA conjugates are used. This approach may face some practical limitation in terms of PNA antisense activity. In this study, we propose a novel RATH-2 peptide-based non-covalent PNA delivery mechanism. We observed RATH-2 shows a favorable mol. interaction with PNA at 16:1 (peptide:PNA) molar ratio resulting in co-centric nanoparticle formation. With this combination, we could achieve as high as 93% cellular delivery of the PNA. The proposed non-covalent RATH:PNA delivery model showed endocytic entrapment free delivery of PNA. The study further demonstrated the therapeutic application of PNA with in vitro antiviral intervention model. Using RATH-2 non-covalent PNA delivery system, we could inhibit 69.5% viral load. The present study demonstrates a cell-penetrating peptide:PNA interaction can lead to nanoparticle formations that facilitated cellular delivery of PNA.

Halder, Moumita team published research on Biomaterials Science in 2022 | 35737-15-6

Halder, Moumita;Bhatia, Yatin;Singh, Yashveer research published 《 Self-assembled di- and tripeptide gels for the passive entrapment and pH-responsive, sustained release of an antidiabetic drug, glimepiride》, the research content is summarized as follows. Diabetes is a global epidemic that poses a severe challenge to public health. The characteristic features of this disease are hyperglycemia and deterioration of the function of pancreatic β-cells, which leads to oxidative stress and organ damage. Glimepiride is used to treat type II diabetes but is associated with side effects, like lower half-life, faster elimination, and hypoglycemia. Self-assembled peptide gels have drawn attention as a drug delivery depot because of their biocompatibility, diverse design, tunable functionality, and dynamic self-assembly properties. In order to overcome the challenge of oxidative stress and side effects associated with the use of glimepiride, we have developed glimepiride-loaded, self-assembled peptide gels from di- and tripeptides employing amino acids with inherent antioxidant properties. Dipeptides, Fmoc-Tyr-Tyr-NH₂ (YY) and Fmoc-Trp-Trp-NH₂ (WW), and a tripeptide, Fmoc-Trp-Trp-His-NH₂ (WWH), were developed and self-assembled into gels. The gels exhibited excellent viscoelastic properties and self-healing abilities, and the presence of β-sheet secondary structures. The dipeptide gels provided a sustained drug release but more drug was released at physiol. pH (7.4) than acidic pH (5 and 6), whereas the tripeptide gel released more drug at acidic pH. The gels showed free radical scavenging activities of more than 90% and were able to decrease the amount of oxidative stress caused by the ROS in HepG2 cells. They were non-toxic to the cell line tested and HepG2 cells treated with the releasate of tripeptide gels showed enhanced glucose uptake. This work for the first time reports the development of glimepiride-loaded self-assembled peptide gels, which can serve as a dynamic, multidimensional biomaterial to reduce oxidative stress, hypoglycemia, and repetitive dosing of drugs in diabetic patients by controlling glimepiride release.

Gou, Sanhu team published research on Journal of Medicinal Chemistry in 2021 | 35737-15-6

Recommanded Product: Fmoc-Trp-OH, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Gou, Sanhu;Li, Beibei;Ouyang, Xu;Ba, Zufang;Zhong, Chao;Zhang, Tianyue;Chang, LinLin;Zhu, Yuewen;Zhang, Jingying;Zhu, Ningyi;Zhang, Yun;Liu, Hui;Ni, Jingman research published 《 Novel Broad-Spectrum Antimicrobial Peptide Derived from Anoplin and Its Activity on Bacterial Pneumonia in Mice》, the research content is summarized as follows. The emergence of multidrug-resistant bacteria has major issues for treating bacterial pneumonia. Currently, anoplin (GLLKRIKTLL-NH₂) is a natural antimicrobial candidate derived from wasp venom. In this study, a series of new antimicrobial peptide (AMP) anoplin analogs were designed and synthesized. The relationship between their biol. activities and their pos. charge, hydrophobicity, amphipathicity, and secondary structure are described. The characteristic shared by these peptides is that pos. charged amino acids and hydrophobic amino acids are severally arranged on the hydrophilic and hydrophobic surface of the α-helix to form a completely amphiphilic structure. To achieve ideal AMPs, below the range of the threshold of the cytotoxicity and hemolytic activity, their charges and hydrophobicity were increased as much. Among the new analogs, A-21 (KWWKKWKKWW-NH₂) exhibited the greatest antimicrobial activity (geometric mean of min. inhibitory concentrations = 4.76μM) against all the tested bacterial strains, high bacterial cell selectivity in vitro, high effectiveness against bacterial pneumonia in mice infected with Klebsiella pneumoniae, and low toxicity in mice (LD₅₀ = 82.01 mg/kg). A-21 exhibited a potent bacterial membrane-damaging mechanism and lipopolysaccharide-binding ability. These data provide evidence that A-21 is a promising antimicrobial candidate for the treatment of bacterial pneumonia.

Gabrielli, V. team published research on Materials Today Chemistry in 2022 | 35737-15-6

Gabrielli, V.;Missale, E.;Cattelan, M.;Pantano, M. F.;Frasconi, M. research published 《 Supramolecular modulation of the mechanical properties of amino acid-functionalized cellulose nanocrystal films》, the research content is summarized as follows. Cellulose nanocrystal (CNC) is a promising building block for the bottom-up assembly of novel lightweight renewable materials. The ability to engineer the interfacial properties of CNC is of paramount importance to develop assembled materials for various applications; yet it remains a challenge to manipulate the supramol. interactions within the cellulosic nanomaterials in a controlled manner. In this context, we demonstrate in this article how the assembly and mech. properties of cellulose thin films can be controlled by manipulating the interfacial interactions of TEMPO-oxidized cellulose nanocrystals (TOCNCs) grafted with two different amino acids, arginine and tryptophan. The amino acid grafting onto the cellulose scaffold was confirmed in aqueous solutions by ¹H NMR spectroscopy and in solid form by FTIR and XPS techniques. The surface functionalization of TOCNCs with simple cationic and aromatic groups provides a strategy for tuning the assembly of the nanostructures based on different supramol. crosslinking interactions, including hydrogen bonds, π-π stacking, and cation-π interactions. In particular, we show that nanocellulose chains crosslinked by the non-covalent cation-π interactions lead to the formation of a laminated superstructure with high deformation and load standing capabilities. Our work provides a versatile strategy for tuning the surface properties of nanocellulose and represents an important step toward the development of sustainable materials with tailored mech. properties, which will enable a wider application range of this building block all the way from tissue-engineering scaffolds to flexible devices.