Crystallographic Analysis of Short Helical Peptides Containing Homologs of Phenylalanine.

Interactions between aromatic side chains of amino acids stabilize the fold and assembly of short peptides. The aromatic π…π and C-H…π interactions have been widely explored in the design of short peptides with specific folding and aggregation patterns. In the present study, we investigated the effect of homologated phenylalanine side chains on the conformation and assembly of peptide helices through X-ray crystallographic structure determination and analysis of five pentapeptides.

Incorporation of phenylcarbonyl groups in the sidechain: A tool to induce ordered assembly of peptides on surfaces.

The possibility of introducing various functionalities on peptides with relative ease allows them to be used for molecular applications. However, oligopeptides prepared entirely from proteinogenic amino acids seldom assemble as ordered structures on surfaces. Therefore, sidechain modifications of peptides that can increase the intermolecular interactions without altering the constitution of a given peptide become an attractive route to self-assembling them on surfaces.

Acknowledging the use of botanicals to treat diabetic foot ulcer during the 21 century: A systematic review.

Background: Diabetic foot ulcer (DFU) is a serious health issue of diabetes mellitus that affects innumerable people worldwide. Management and treatment of this complication are challenging, especially for those whose immune system is weak.

Aim: To discuss the plants and their parts used to heal DFU, along with the mode of their administration in diabetic patients.

Synthesis of peptides containing oxo amino acids and their crystallographic analysis.

An isolated uncharged hydrogen bond acceptor such as the carbonyl functionality of an aldehyde or a keto group is absent in natural amino acids. Although glutamine and asparagine are known to hydrogen bond through the amide carbonyl group in their side chains, they also possess the amide NH group, which can act as a hydrogen bond donor. This makes the structural study of peptides containing an oxo residue, with an isolated carbonyl group in the side chain, interesting.