Specific Adhesion of Peptides on Semiconductor Surfaces in Experiment and Simulation

TL;DR

This study investigates how peptides adhere to semiconductor surfaces, examining their self-assembly, clustering, and conformational phases through experiments and simulations, revealing the influence of surface and peptide polarity on adhesion behavior.

Contribution

It introduces a combined experimental and simulation approach to understand peptide adhesion on semiconductor surfaces, highlighting the effects of polarity and hydrophobicity on adhesion and clustering.

Findings

Peptide surface coverage varies by a factor of 25 based on polarity.

Low adhesion leads to large, soft clusters with high contact angles.

Simulated phase diagram shows temperature and solvent effects on peptide phases.

Abstract

We report on self-assembly, clustering, and conformational phases of peptides on inorganic semiconductor surfaces. The peptide-covered surface fraction can differ by a factor of 25, depending mainly on surface and peptide polarity. Low adhesion induces large and soft clusters, which also have high contact angles to the surface. Direct surface adhesion of a peptide molecule competes with forming molecular aggregates which offer an overall reduced surface contact. Simulating a simple hybrid model yields a pseudophase diagram with a rich, temperature and solvent-quality dependent variety of subphases which are specific to the hydrophobicity and polarity of the considered substrates.