Protein and Peptide Letters - Volume 18, Issue 3, 2011

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 p Read More

The relaxin peptide family in humans consists of seven members, relaxin-1, -2 and -3 and insulin- like (INSL) peptides 3, 4, 5 and 6. It is an offshoot of the large insulin superfamily. Each member consists of two chains, commonly referred to as A and B, which are held together by two inter-chain disulfide bonds and another intra-chain disulfide bond present within the A chain. The cysteine residues present in each chain, together Read More

Under certain in vitro conditions, α-synuclein, an abundant 14kDa presynaptic intrinsically disordered protein involved in the pathogenesis of Parkinson's disease (PD), forms amyloid fibrils which resemble those found in Lewy bodies of PD patients. However, a substantial fraction of α-synuclein molecules (10-20%) does not form fibrils during fibrillation and exists in a form of soluble oligomers. In this study, we examine Read More

With the emergence of multi-drug resistant (MDR) and extensively drug resistant (XDR) Mycobacterium tuberculosis (Mtb), new classes of anti-mycobacterial agents with very different modes of action compared to classical antibiotics, are urgently needed. In this study, a series of 26-residue, amphipathic α-helical antimicrobial peptides consisting of all D-amino acid residues and synthetic human L-LL37 (L-enantiomer) Read More

Stability and unfolding of mammalian and microbial α-amylases have been intensively investigated. However, there is only limited information available on the structural stability of plant α-amylases, namely of the two isoenzymes from barley AMY1 and AMY2, of the α-amylase from mung bean (Vigna radiata), and of the α-amylase from malted sorghum (Sorghum bicolor). We report here the stability of soybean α-amylase Read More

Conotoxins are small disulfide-rich peptides that are invaluable channel-targeted peptides and target neuronal receptors. They show prospects for being potent pharmaceuticals in the treatment of Alzheimer's disease, Parkinson's disease, and epilepsy. Accurate and fast prediction of conotoxin superfamily is very helpful towards the understanding of its biological and pharmacological functions especially in the post-genomic era. Read More

Here we present a 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. Using atomic force microscopy the fibrillisation of these peptides at the liquid/solid interface utilizing ordered crystalline substrates has been investigated. Our results demonstrate that the assembly pathway at the liquid/solid interface enables only the form Read More

The small heat shock protein SsHSP14.1 from the hyper-thermophilic archeaon, Sulfolobus solfataricus (S. solfataricus) was able to protect proteins from thermal aggregation and prevent enzymes from heat induced inactivation. According to the 3D (dimensional) structural model of SsHSP14.1 developed by us before, the region L5-7 (β5-β7, 68-82 residues) plays an important role for the oligomerization of SsHSP14.1 and its cha Read More

A new, fast, simple and cost-effective sensing device for monitoring H2S has been developed. Proof-of-principle results showing that a commercial and cheap Myoglobin (Mb) can be successfully used as a biological probe for a fluorescence biosensor for H2S detection are reported. Two different commercial labels Cy3 and Atto620 were selected for this study. A high selectivity for detecting H2S against other thiols was found. The Read More

Vibriolysin is among several zinc metalloproteases produced by Vibrio cholerae. It is involved in the molecular pathogenicity of cholera. Here, we cloned and expressed full-length vibriolysin gene from V. cholerae. Electrophoretic and mass spectrometric data showed that the N-terminal pro-peptide was removed from pro-vibriolysin generating a 45- kDa segment containing the metalloprotease plus the C-terminal domains, a Read More

Botulinum neurotoxins (BoNTs) are highly potent toxins that inhibit neurotransmitter release from peripheral cholinergic synapses. The gene for encoding the full length light chain with HCC (binding) domain of Clostridium botulinum neurotoxin A was synthesized and cloned into a bacterial expression vector pQE30-UA and produced as an Nterminally six-histidine-tagged fusion protein (rBoNT/A LC-HCC). This protein was exp Read More

The combination of several drugs is often necessary, especially during long-term therapy. A competitive binding of the drugs can cause a decrease of the amount of drugs actually bound to the protein and increase the biologically active fraction of the drug. The aim of this study has been to analyze the interactions of tamoxifen (TMX) and aspirin (ASA) with human serum albumin (HSA) and to evaluate the mechanism of a si Read More

Temperature dependence of the α-helix conformation of bee venom melittin in methanol-water mixed solvents has been examined by NMR, in order to elucidate conformation stability and a phase diagram. At high methanol concentration of 100 - ca. 80 wt.%, melittin forms a full α-helix conformation in the temperature range from 25 °C to 60 °C. At intermediate methanol concentration of ca. 80 - ca. 25 wt.%, it undergo Read More