Editorial (Special Board Members Issue)

This is the third issue of Protein & Peptide Letters in which all the manuscripts have been contributed by the members of the Editorial Advisory Board of the journal. The papers included here demonstrate the wide variety of research areas covered by the Editorial Board. The field of proteins & peptides is very broad, encompassing wide areas of current chemistry, biology, biomaterials and related areas. This is true because proteins and peptides can be found in all living system and are responsible for both form and function, i.e., structural protein and enzymes, to name just two examples. The accelerating discoveries of the roles of these molecules in the pathology of disease and in new biomaterials with useful promise to expand the field even further. I am sure you will find papers in this issue quite interesting to read: The paper by Dr. John Wade et al. discusses the relaxin peptide family in humans consisting of seven members: relaxin-1, -2 and -3 and insulin-like (INSL) peptides 3, 4, 5 and 6. In the paper by Dr. Vladimir Uversky et al. it has been found that the soluble oligomers are important players in the multipathway aggregation of α-synuclein and should be taken into account in studies on the molecular mechanisms of this protein Dr. Robert Hodges and colleagues describe a series of 26-residue, amphipathic α-helical antimicrobial peptides consisting of all D-amino acid residues. A synthetic human L-LL37 (L-enantiomer) and D-LL37 (D-enantiomer) were investigated against M. tuberculosis susceptible strain (H37Rv) and a clinical multi-drug resistant strain (Vertulo). Structural stability of soybean (Glycine max) α-amylase by Dr. Arvind Kayastha et al. reports the stability of soybean α- amylase (GMA) against elevated temperatures and chemical denaturants (GndHCl) by employing circular dichroism and fluorescence spectroscopy. Dr. Hong-Bin Shen et al. developed a novel approach called PredCSF for predicting the conotoxin superfamily from the amino acid sequence directly based on fusing different kinds of sequential features by using modified one-versus-rest SVMs. In the paper by Dr. Saul Tendler and colleagues study of five analogues of a fragment from the shaft domain of the adenovirus fibre protein that readily form fibrils under a range of conditions is presented. Dr. Kuo-Chen Chou et al. describes that the region L5-7 (β5-β7, 68-82 residues) plays an important role for the oligomerization of SsHSP14.1 and its chaperone function. Here, to validate the findings, an in-depth investigation was conducted of both the wild type SsHSP14.1 and its deletion mutant DEL75-79. With E. coli proteins and bromelain as substrate, the deletion mutant DEL75-79 can protect them from thermo-aggregating as effectively as the wild protein. Dr. Sabato D'Auria et al. found that commercial and cheap Myoglobin (Mb) can be successfully used as a biological probe for a fluorescence biosensor for H2S detection. I appreciate efforts from the Editorial Office and wish them and journal all the best.