Effect of Chain Topology on the Self-Organization and Dynamics of Block Copolypeptides: From Diblock Copolymers to Stars

• Published in: Biomacromolecules Vol. 9; no. 7; pp. 1959 - 1966
• Main Authors: Gitsas, A, Floudas, G, Mondeshki, M, Butt, H.-J, Spiess, H. W, Iatrou, H, Hadjichristidis, N
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-07-2008
• Subjects: Aminoacid polymers; Applied sciences; Exact sciences and technology; Peptides - chemistry; Physicochemistry of polymers; Polyglutamic Acid - analogs & derivatives; Polylysine - analogs & derivatives; Polymers - chemistry; Protein Structure, Secondary; Synthetic biopolymers; Linear copolymer; Aminoacid copolymer; Gamma benzyl glutamate copolymer; Nanostructure; Experimental study; Dielectric relaxation; Star copolymer; Solid state; Domain structure; Supramolecular structure; Diblock copolymer; Helical structure; Block copolymer; Comparative study; Conformation
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm800221n

The effect of chain topology on (i) the peptide secondary structure, (ii) the nanophase self-assembly, and (iii) the local segmental and global peptide relaxations has been studied in a series of model diblock and 3-arm star copolypeptides of poly(ϵ-carbobenzyloxy-l-lysine) (PZLL) and poly(γ-benzyl-l-glutamate) (PBLG) with PZLL forming the core. Diblock copolypeptides are nanophase separated with PBLG and PZLL domains comprising α-helices packed in a hexagonal lattice. Star copolypeptides are only weakly phase separated, comprising PBLG and PZLL α-helices in a pseudohexagonal lattice. Phase mixing has profound consequences on the local and global dynamics. The relaxation of the peptide secondary structure speeds up, and the helix persistence length is further reduced in the stars, signifying an increased concentration of helical defects.