Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides

Ariawan, A. Daryl; Sun, Biyun; Wojciechowski, Jonathan P.; Lin, I-An; Du, Eric Y.; Goodchild, Sophia C.; Cranfield, Charles G.; Ittner, Lars M.; Thordarson, Pall; Martin, Adam D.

doi:10.1039/d0sm00320d

Cited by 5 publications

(4 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fmoc-tetrapeptides Fmoc-XXFF where X indicates a polar residue, i.e., charged D, E, R or K or neutral N or Q have been prepared and studied . Fibrils were observed for all conjugates containing charged residues but not those with neutral N or F. Hydrogels were observed for all conjugates via pH switch using GdL.…”

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

“…Fibrils were observed for all conjugates containing charged residues but not those with neutral N or F. Hydrogels were observed for all conjugates via pH switch using GdL. The cytotoxicity was also examined along with interactions with tethered lipid membranes . Fmoc-tetrapeptides DAAR or DGGR contain dialanine or diglycine substrates for enzymes including chymotrypsin, elastase or thermolysin.…”

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

“…The cytotoxicity was also examined along with interactions with tethered lipid membranes. 91 Fmoc-tetrapeptides DAAR or DGGR contain dialanine or diglycine substrates for enzymes including chymotrypsin, elastase or thermolysin. This has been used in an enzyme detection system based on covalent linking of the Fmoc peptides to PEGA (PEG/acrylamide copolymer) particles containing dextran which swell due to enzyme cleavage (which leads to D/R zwitterion formation) and dextran release.…”

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

See 2 more Smart Citations

Self-Assembly, Bioactivity, and Nanomaterials Applications of Peptide Conjugates with Bulky Aromatic Terminal Groups

Hamley

2023

ACS Appl. Bio Mater.

View full text Add to dashboard Cite

The self-assembly and structural and functional properties of peptide conjugates containing bulky terminal aromatic substituents are reviewed with a particular focus on bioactivity. Terminal moieties include Fmoc [fluorenylmethyloxycarbonyl], naphthalene, pyrene, naproxen, diimides of naphthalene or pyrene, and others. These provide a driving force for self-assembly due to π-stacking and hydrophobic interactions, in addition to the hydrogen bonding, electrostatic, and other forces between short peptides. The balance of these interactions leads to a propensity to selfassembly, even for conjugates to single amino acids. The hybrid molecules often form hydrogels built from a network of β-sheet fibrils. The properties of these as biomaterials to support cell culture, or in the development of molecules that can assemble in cells (in response to cellular enzymes, or otherwise) with a range of fascinating bioactivities such as anticancer or antimicrobial activity, are highlighted. In addition, applications of hydrogels as slow-release drug delivery systems and in catalysis and other applications are discussed. The aromatic nature of the substituents also provides a diversity of interesting optoelectronic properties that have been demonstrated in the literature, and an overview of this is also provided. Also discussed are coassembly and enzyme-instructed self-assembly which enable precise tuning and (stimulusresponsive) functionalization of peptide nanostructures.

show abstract

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

Section: Fluorenylmethyloxycarbonylmentioning

confidence: 99%

See 1 more Smart Citation

Self-Assembly, Bioactivity, and Nanomaterials Applications of Peptide Conjugates with Bulky Aromatic Terminal Groups

Hamley

2023

ACS Appl. Bio Mater.

View full text Add to dashboard Cite

show abstract

“…Short peptides and their analogues have been attracting great interest in recent years as building blocks for soft matter. [1][2][3][4][5][6][7] They offer several advantages over other molecular classes, such as ease of preparation and scale-up, low cost, inherent biocompatibility and biodegradability, as well as the possibility to encode biological messages. 8 In particular, it has been shown that a sequence as short as a tripeptide possesses, on average, the ideal number of non-carbon atoms required to maximise ligand-receptor interactions to develop drug-like molecules.…”

Section: Introductionmentioning

confidence: 99%

Supramolecular hydrogels from unprotected dipeptides: a comparative study on stereoisomers and structural isomers

et al. 2020

View full text Add to dashboard Cite

show abstract

Single Amino‐Acid Based Self‐Assembled Biomaterials with Potent Antimicrobial Activity

Misra

Mukherjee

Ghosh

et al. 2021

Chemistry A European J

View full text Add to dashboard Cite

The design and development of soft biomaterials based on amino acid and short-peptide have gained much attention due to their potent biomedical applications. A slight alteration in the side-chain of single amino acid in a peptide or protein sequence has a huge impact on the structure and function. Phenylalanine is one of the most studied amino acids, which contains an aromatic phenyl group connected through a flexible À CH 2 À unit. In this work, we have examined whether flexibility and aromatic functionality of phenylalanine (Phe) are important in gel formation of model gelator Fmoc-Phe-OH or not. To examine this hypothesis, we synthesized Fmoc-derivatives of three analogues unnatural amino acids including cyclohexylalanine, phenylglycine, and homophenylalanine; which are slightly varied from Phe. Interestingly, all these three new analogues formed hydrogels in phosphate buffer at pH 7.0 having different gelation efficacy and kinetics. This study suggests that the presence of aromatic side-chain and flexibility are not mandatory for the gelation of this model gelator. Newly synthesized unnatural amino acid derivatives have also exhibited promising antimicrobial activity towards gram-positive bacteria by inhibiting cellular oxygen consumption. We further determined the biocompatibility of these amino acid derivatives by using a hemolysis assay on human blood cells. Overall studies described the development of single amino acid-based new injectable biomaterials with improved antimicrobial activity by the slight alteration in the side-chain of amino acid.

show abstract

Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides

Abstract: The incorporation of polar amino acids into the Fmoc-FF motif yields tetrapeptide hydrogels whose biocompatibility in the gel state is inversely proportional to their biocompatibility in the solution state.

Cited by 5 publications

References 46 publications

Self-Assembly, Bioactivity, and Nanomaterials Applications of Peptide Conjugates with Bulky Aromatic Terminal Groups

Self-Assembly, Bioactivity, and Nanomaterials Applications of Peptide Conjugates with Bulky Aromatic Terminal Groups

Supramolecular hydrogels from unprotected dipeptides: a comparative study on stereoisomers and structural isomers

Single Amino‐Acid Based Self‐Assembled Biomaterials with Potent Antimicrobial Activity

Contact Info

Product

Resources

About