AMBROGGIO ERNESTO
Artículos
Título:
Reversing the peptide sequence impacts on molecular surface behaviour
Autor/es:
AMBROGGIO ERNESTO ESTEBAN; CARUSO BENJAMIN; VILLARREAL MARCOS ARIEL; RAUSSENS VINCENT; FIDELIO GERARDO DANIEL
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2015 vol. 139 p. 25 - 25
Resumen:
he protein?s primary structure has all the information for specific protein/peptide folding and, in many cases, can define specific amphiphilic regions along molecules that are important for interaction with membranes. In order to shed light on how peptide sequence is important for the surface properties of amphiphilic peptides, we designed three pairs of peptides with the following characteristics: (1) all molecules have the same hydrophobic residues; (2) the couples differ from each other in their hydrophilic amino acids: positively, negatively and non-charged; (3) each pair has the same residues (same global molecular hydrophobicity) but the primary structure is reversed in comparison to its partner (retro-isomer), giving a molecule with a hydrophilic N or C-terminus and a hydrophobic C or N-terminus. Using the Langmuir monolayer approach, we observed that sequence reversal has a central role in the lateral stability of peptide monolayers, in the ability of the molecules to partiti