Acyl peptide surfactant

Of the PBS, amino acid surfactants have been the subject of many studies, primarily on their applications as pharmaceuticals, biomedicals, cosmetics, household cleaners, and antimicrobial agents. On the other hand, except for few fragmentary reports, experimental work on peptide surfactants is relatively scanty. Both amino acid surfactants and peptide surfactants are interesting biocompatible compounds that contain amino acid or dipeptide as the hydrophilic part and a long hydrocarbon chain as the hydrophobic part. The hydrocarbon chain can be introduced through acyl, ester, amide, or alkyl linkage. 

Applications. Acyl peptides are mild surfactants designed for the personal care area they are especially used in shampoos because of their substantivity on the keratin of hair and, therefore, they effectively deliver the expected benefits of conditioning agents, (c) Acyl Sarcosides... 

High-molecular-weight protein-fatty acid condensates are reported to be more effective than acylated derivatives of smaller peptide in increasing the skin and eye tolerability of different anionic tenside, as evaluated by the red blood cell test (127) and quatemized derivatives also reported to possess anti-irritant properties when included in anionic-based formulations the mucous membrane compatibility of sodium laureth sulfate, as determined by the Draize test, can be increased about fourfold, by replacing of one-third of the surfactant with a lauryldimonium hydroxypropyl hydrolyzed collagen (128). 

Condensation of hydrolyzed proteins with fatty acid groups determines reduction of the skin and eye compatibility, resulting from the increase of their amphiphilic character the skin/eye tolerability of acylated proteins is reported to increase with the average length of the peptide moiety (127). Quaternized derivatives are generally less compatible than fatty acid condensates (128). The irritation potential of protein-surfactant complexes is intermediate between those of the parent protein and the pure tenside. 

FIG. 2 Structures of lipopeptidic surfactants synthesized from arginine (a) pure lauroyl-L-arginine dipeptides (b) polydisperse Al -acyl-L-arginine dipeptides (c) poly-disperse Al -acyl-L-arginine peptides. 

Water-soluble antimicrobial Upopeptides have been prepared by the condensation of amino acids or peptides to lV -acyl arginine residues with suitable lipophilic contents. Our data suggest that such arginine lipopeptidic surfactants have value as soft preservatives in cosmetic, food, and dermopharmaceutical formulations, as well as being tools for fundamental research. 

Pulmonary surfactant protein C (SP-C) is a small hydrophobic peptide. The effect of acylation of SP-C on its structure and function was reported by Haagsman et al. [146] using the Whilelmy plate method and CD spectra measurement. Also, SP-C-induced bilayer interaction was studied via the lipid mixing method by the use of fluorescence spectra of pyrene-PC labeled vesi-... 

One important milestone in our research is the design and development of new amino acid-based surfactants with antimicrobial properties, which mimic natural amphiphilic cationic peptides [42,43]. To this end, Lys and Arg derivatives of long-chain A -acyl, COO-ester, and A-alkyl amide have been prepared. In particular, the A -acylarginine methyl ester derivatives series 1 (Scheme 1) have turned out to be an important class of cationic surface active compounds with a wide bactericidal activity, high biodegradability, and low toxicity profile. We have shown that essential structural factors for their antimicrobial activity include both the length of the fatty residue (akin with their solubility and surface activity) and the presence of the protonated guanidine function [43,44]. 

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