title: Propensity of Self-Assembled Leucine-Lysine Diblock Copolymeric α-Helical Peptides To Remain in Parallel and Antiparallel Alignments in Water.
abstract: Molecular dynamics simulation study of α-helical diblock copolypeptides preassembled in parallel and antiparallel alignments in water are presented. The assembled peptide lamellar structures were not disrupted even after performing three-step simulation protocols. Primarily hydrogen bonds between peptide are responsible for the stability. The analysis of the trajectory also suggests that water plays a significant role in favoring self-assembly. We have detected continuous hydrogen bonded network structure, which is further responsible for the stability of the lamellar structures. We have performed a detailed analysis of the hydrogen bonded network structure and its length. Further, free energy calculations revealed that the degree of stability for both lamellae are similar. The present study provides structural insight into the stability of self-assembled structures of block copolypeptides.
authors.affiliation: Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune - 411008, India.
authors.forename: Sujit
authors.initials: S
authors.lastname: Sarkar
authors.affiliation: Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune - 411008, India.
authors.forename: Prithvi Raj
authors.initials: PR
authors.lastname: Pandey
authors.affiliation: Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune - 411008, India.
authors.forename: Sudip
authors.initials: S
authors.lastname: Roy
mesh_terms: D006860:Hydrogen Bonding; D007930:Leucine / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D010455:Peptides; D014867:Water; D007930:Leucine; D008239:Lysine