Abstract

The lateral organization and clustering of transmembrane peptides are critical determinants of their biological function, including their roles in membrane fusion, ion channel formation, and antimicrobial activity. This study investigates the fundamental physical principles governing the self-assembly of these membrane-spanning molecules. We present a theoretical model to analyze the **lateral interaction of cylindrical transmembrane peptides** embedded within a lipid bilayer, employing a **one-dimensional approximation** to simplify the complex three-dimensional environment. The primary objective is to quantify the potential of mean force between two such peptides as a function of their separation distance. Our approach considers contributions from membrane elastic deformations, hydrophobic mismatch, and electrostatic forces. Key findings reveal that the interaction potential is highly sensitive to the peptide radius and the membrane's elastic properties, exhibiting a complex profile with both short-range attractive wells and long-range repulsive barriers. This theoretical framework provides crucial insights into the mechanisms driving peptide-peptide recognition and clustering, which are essential for understanding the stability and function of multi-subunit membrane protein complexes and for the rational design of novel antimicrobial peptides and drug delivery systems.