Self‐assembly of t‐butyloxycarbonyl protected dipeptide methyl esters composed of leucine, isoleucine, and valine into highly organized structures from alcohol and aqueous alcohol mixtures. Issue 6 (20th November 2017)

• Record Type: Journal Article
• Authors: Subbalakshmi, Chivukula; Basak, Pratyay; Nagaraj, Ramakrishnan
• Is Part Of: Biopolymers. Volume 108:Issue 6(2017)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-11-20
• Subjects: circular dichroism -- electron microscopy -- hydrophobic peptides -- nanostructures -- powder X‐ray diffraction -- self‐assembly; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.23033
• Languages: English
• ISSNs: 0006-3525

Abstract

Abstract: Short peptides composed of phenylalanine and sequences derived from amyloidogenic peptides have the ability to self‐assemble to form nanostructures including hydrogels. The self‐assembly of peptides composed of only hydrophobic amino acids and aliphatic protecting groups have not been investigated in detail. We have examined various aspects of nanostructures formed by N‐terminal t‐butyloxycarbonyl‐protected aliphatic dipeptide methyl esters dissolved in various solvents. Scanning electron microscopic images indicate that depending on the sequence, position of the amino acid and solvent of dissolution, the peptides self‐assemble into superstructures such as nanotubes and needles particularly from aqueous mixtures of organic solvents. Crystallization was not required for self‐assembly into nanostructures. Circular dichroism and attenuated total internal reflection fourier transform infrared spectroscopy studies indicate that the peptides adopt β‐conformation in the superstructures both in solution and solid state. The nanostructures composed of entirely aliphatic moieties have the ability to bind to aromatic dyes such as Rhodamine 6G, Nile red and Congo red. They also bind to Thioflavin T although the structures do not resemble amyloid fibrils. The powder X‐ray diffraction patterns suggest distinctive packing of the monomers. These structures are stabilized by intermolecular hydrogen bonds and hydrophobic interactions resulting in superstructures containing long distance order and were devoid of hemolytic activity. Abstract :