2022
DOI: 10.1039/d2sm00562j
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Amino acid containing amphiphilic hydrogelators with antibacterial and antiparasitic activities

Abstract: Here we present a series of peptide amphiphiles which form hydrogels based on beta-sheet nanofibril networks, several of which have very promising anti-microbial and anti-parasitic activities, in particular against multiple...

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Cited by 9 publications
(8 citation statements)
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“…The molecular structure of sPAs closely resembles the reported PA, comprising a hydrophobic domain, aromatic core, self‐assembling region, and a linear amino acid with minimal side chain effects as a hydrophilic epitope. Further simplification led to the design of very short peptide amphiphiles (vsPA), [13] considered as the smallest lipopeptide and a shorter analogue of the same. The right panel depicts concentration‐dependent assembly followed by AuNPs formation for potential applications.…”
Section: Figurementioning
confidence: 99%
See 1 more Smart Citation
“…The molecular structure of sPAs closely resembles the reported PA, comprising a hydrophobic domain, aromatic core, self‐assembling region, and a linear amino acid with minimal side chain effects as a hydrophilic epitope. Further simplification led to the design of very short peptide amphiphiles (vsPA), [13] considered as the smallest lipopeptide and a shorter analogue of the same. The right panel depicts concentration‐dependent assembly followed by AuNPs formation for potential applications.…”
Section: Figurementioning
confidence: 99%
“…[6] Therefore, the potential application of these peptides across various fields underscores the necessity for continuous comprehensive investigations to gauge their feasibilities and motivates us to miniaturize the structural feature that governs the self-assembly by focusing primarily on three segments, (i) lipid segment or length of alkyl chain (ii) self-assembling aromatic components (iii) requirement of hydrophilic component as C-terminus epitope. [10,11] Such rational design [12] is a necessary building block for the bottom-up fabrication of nanomaterial and possesses the simplicity with the versatility of small peptide [13] conjugate molecules. Such kind of molecules fall under the lipopeptide [14,15] category where the desired peptide sequence is conjugated at appropriate positions.…”
mentioning
confidence: 99%
“…19 These peptide gelators form hydrogels with micro-and nanofibril network structures under appropriate conditions through the selfassembly of individual molecules by using various noncovalent interactions including hydrogen bonding, p-p interactions, van der Waals interactions, hydrophobic interactions and others. [20][21][22][23][24] These hydrogels have a wide range of applications in the biomedical field, such as sustained release of drugs and important biomolecules, [25][26][27][28] drug delivery, 25,29 cell culture, 27 tissue engineering, 1,29 wound healing, 19,32 and antimicrobial, [30][31][32][33][34][35][36][37][38][39][40] antiparasitic 37,42 and anticancer agents. [41][42][43][44][45][46][47][48] The self-assembled nanostructures show a remarkably increased bioactivity compared to the unassociated peptide molecules.…”
Section: Introductionmentioning
confidence: 99%
“…In recent years, peptide-based hydrogels , have been developed as biomaterials that act as antimicrobial agents for the treatment of infectious diseases . Several kinds of hydrogels have been reported so far, , but there are few peptide-based low molecular weight hydrogels that inherently show antimicrobial activity. Polycation moieties have antimicrobial properties, but often show a certain level of toxicity to mammalian cells . Mainly antibacterial activities of peptide hydrogels with positively charged ammonium ion based molecules are well known.…”
Section: Introductionmentioning
confidence: 99%