Hydrophobic dipeptides: the final piece in the puzzle

Abstract

The crystal structure of L-valyl-L-leucine acetonitrile solvate presented here adds to 24 previously reported structures of dipeptides constructed from the five nonpolar amino acids L-alanine, L-valine, L-isoleucine, L-leucine and L-phenylalanine. It thus constitutes the final piece in the 5 × 5 puzzle of hydrophobic dipeptide structures. This opportunity is taken to review the crystal packing arrangements and hydrogen-bonding preferences of a rather unique group of substances, with updated information on the various hydrogen-bonding patterns and the associated peptide conformations.

Molecular Dynamics Simulation Study of the Self-Assembly of Phenylalanine Peptide Nanotubes

“…It is known that diphenylalanine dipeptides (FF or (Phe) 2 ) are also formed from such a phenylalanine amino acid (F or Phe) and are assembled into similar peptide nanotubes [ 12 , 17 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 ]. Diphenylalanine dipeptide FF and peptide nanotubes (PNTs) based on it (FF PNTs) are currently quite well studied, as they are of considerable interest due to their special structural and physical properties important in various applications [ 17 , 44 , 45 , 46 , 47 ].…”

“…Diphenylalanine dipeptide FF and peptide nanotubes (PNTs) based on it (FF PNTs) are currently quite well studied, as they are of considerable interest due to their special structural and physical properties important in various applications [ 17 , 44 , 45 , 46 , 47 ]. These self-assembled FF PNTs are biocompatible [ 12 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ] and exhibit excellent mechanical [ 33 , 34 ], chemical and thermal stability [ 35 ] in biomedical applications [ 12 , 17 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 ], and they have interesting electronic [ 36 ], optical [ 37 , 38 , 39 , 40 ] and pyroelectric [ 41 ] properties, as well as strong polarization [ 12 , 17 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 ] and exceptional piezoelectric effect […”

Self-assembly of Boc-p-nitro-l-phenylalanyl-p-nitro-l-phenylalanine and Boc-l-phenylalanyl-l-tyrosine in solution and into piezoelectric electrospun fibers

“…These structures result from stacking of molecules through the formation of intermolecular hydrogen bonds between functional groups in the peptide backbone. 2 The most studied self-assembled system is L-phenylalanyl-Lphenylalanine or diphenylalanine (hereafter PhePhe) 3 which is formed by the self-assembly of the aromatic dipeptide into NTs and other nanostructures, 4 such as nanowires 5 and nanorods, 6 depending on the experimental conditions such as pH and temperature. PhePhe NTs have been integrated in devices for electronic and biosensing applications.…”

Structures and Properties of the Self-Assembling Diphenylalanine Peptide Nanotubes Containing Water Molecules: Modeling and Data Analysis

“…It is important that their structural and physical properties turn out to be dependent on the chirality of the original molecules of amino acids and dipeptides [ 29 , 30 , 31 , 32 ]. In many cases, water molecules also appear in the internal hydrophilic cavity of such PNTs [ 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 ]. They affect the physical properties of PNT and largely determine their changes.…”