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The effect of end‐group substitution on surface self‐assembly of peptides
Author(s) -
Dolid Alona,
Reches Meital
Publication year - 2019
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3212
Subject(s) - biofouling , tripeptide , peptide , chemistry , adhesion , dipeptide , staphylococcus epidermidis , coating , bacteria , stereochemistry , organic chemistry , biochemistry , membrane , staphylococcus aureus , biology , genetics
Biofouling, the undesirable accumulation of organisms onto surfaces, affects many areas including health, water, and energy. We previously designed a tripeptide that self‐assembles into a coating that prevents biofouling. The peptide comprises three amino acids: DOPA, which allows its adhesion to the surface, and two fluorinated phenylalanine residues that direct its self‐assembly into a coating and acquire it with antifouling properties. This short peptide has an ester group at its C‐terminus. To examine the importance of this end group for the self‐assembly and antifouling properties of the peptide, we synthesized and characterized tripeptides with different end groups (ester, amide, or carboxylic group). Our results indicate that different groups at the C‐terminus of the peptide can lead to a change in the peptide assembly on the surface and its adsorption process. However, this change only affects the antifouling properties of the coating toward Gram‐positive bacteria ( Staphylococcus epidermidis ), whereas Gram‐negative bacteria ( Escherichia coli ) are not affected.