Novel short antimicrobial peptide isolated from Xenopus laevis skin
In this study, a novel short antimicrobial peptide was purified from Xenopus laevis skin and characterised through reversed‐phase high‐performance liquid chromatography, Edman degradation and matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry. The peptide was composed of six amino acids with a sequence of DEDLDE and thus named X. laevis antibacterial peptide‐P2 (XLAsp‐P2). Transmission electron microscopy revealed that this peptide showed potential antimicrobial abilities against bacteria by damaging the bacterial cell membrane. XLAsp‐P2 maybe inhibit bacterial growth by binding to...
Source: Journal of Peptide Science - February 28, 2017 Category: Biochemistry Authors: Yu Zhang, Songcai Liu, Siming Li, Yunyun Cheng, Linyan Nie, Gang Wang, Chen Lv, Wenzhen Wei, Cheng Cheng, Feng Hou, Linlin Hao Tags: Research Article Source Type: research
Peptides: recent developments and future directions at the 15th Naples workshop on bioactive peptides
(Source: Journal of Peptide Science)
Source: Journal of Peptide Science - February 28, 2017 Category: Biochemistry Authors: Giancarlo Morelli Tags: Editorial Source Type: research
Issue information
(Source: Journal of Peptide Science)
Source: Journal of Peptide Science - February 28, 2017 Category: Biochemistry Tags: Issue Information Source Type: research
Centipede venom peptide SsmTX ‐I with two intramolecular disulfide bonds shows analgesic activities in animal models
Pain is a major symptom of many diseases and results in enormous pressures on human body or society. Currently, clinically used analgesic drugs, including opioids and nonsteroidal anti‐inflammatory drugs, have adverse reactions, and thus, the development of new types of analgesic drug candidates is urgently needed. Animal venom peptides have proven to have potential as new types of analgesic medicine. In this research, we describe the isolation and characterization of an analgesic peptide from the crude venom of centipede, Scolopendra subspinipes mutilans. The amino acid sequence of this peptide was identical with SsmTX...
Source: Journal of Peptide Science - February 28, 2017 Category: Biochemistry Authors: Ying Wang, Xiaojie Li, Meifeng Yang, Chunyun Wu, Zhirong Zou, Jing Tang, Xinwang Yang Tags: Research Article Source Type: research
Aza ‐amino acid scanning of chromobox homolog 7 (CBX7) ligands
An aza‐amino acid scan of peptide inhibitors of the chromobox homolog 7 (CBX7) was performed to study the conformational requirements for affinity to the methyllysine reader protein. Twelve azapeptide analogues were prepared using three different approaches employing respectively N‐(Fmoc)aza‐amino acid chlorides and submonomer azapeptide synthesis to install systematically aza‐residues at the first four residues of the peptide, as well as to provide aza‐lysine residues possessing saturated and unsaturated side chains. The aza‐peptide ligands were evaluated in a chromobox homolog 7 binding assay, providing usefu...
Source: Journal of Peptide Science - February 20, 2017 Category: Biochemistry Authors: Mariam Traor é, Michael Gignac, Ngoc‐Duc Doan, Fraser Hof, William D. Lubell Tags: Special Issue Article Source Type: research
Issue information
(Source: Journal of Peptide Science)
Source: Journal of Peptide Science - February 16, 2017 Category: Biochemistry Tags: Issue Information Source Type: research
Heterochiral Jun and Fos bZIP peptides form a coiled ‐coil heterodimer that is competent for DNA binding
In this study, stereoisomer‐specific peptides were constructed corresponding to regions of the basic‐leucine‐zipper domains of Jun and Fos proteins. basic‐leucine‐zipper domains consist of an N‐terminal basic domain, which is responsible for DNA binding, and a C‐terminal domain that enables homodimerization or heterodimerization via formation of a coiled‐coil. By combining peptides with different stereochemistries, the d‐l heterochiral Jun‐Fos heterodimer formation induced DNA binding by the basic domains of Jun‐Fos. Our study provides new insight into the interaction between l‐peptide and d‐pepti...
Source: Journal of Peptide Science - February 9, 2017 Category: Biochemistry Authors: Rui Kamada, Natsumi Nakagawa, Taiji Oyama, Kazuyasu Sakaguchi Tags: Special Issue Article Source Type: research
Engineering sortase A by screening a second ‐generation library using phage display
We report the generation and screening of a new sortase library using phage display. The screen yielded sortase A mutants that ligate APxTG and FPxTG motifs instead of the canonical LPxTG sorting sequence. (Source: Journal of Peptide Science)
Source: Journal of Peptide Science - February 9, 2017 Category: Biochemistry Authors: Lena Schmohl, Jan Bierlmeier, Fabian Gerth, Christian Freund, Dirk Schwarzer Tags: Rapid Communication Source Type: research
Development of a strategy for the total chemical synthesis of an allergenic protein: the peach LTP Pru p 3
The possibility to obtain allergenic proteins by means of total chemical synthesis would be a big step forward in the development of cures to food allergy and in the study of the mechanism of allergic reactions, because this would allow to achieve control at the molecular level over the structure of the product and to study its relationship with the allergenic activity in fine details. This is instead not possible by using allergens produced by extraction from natural sources or by recombinant DNA techniques. In this work, we aimed to test for the first time the feasibility of the total chemical synthesis of an allergenic ...
Source: Journal of Peptide Science - February 9, 2017 Category: Biochemistry Authors: Sofie Buhler, Jaap H. Akkerdaas, Thelma A. Pertinhez, Ronald Van Ree, Arnaldo Dossena, Stefano Sforza, Tullia Tedeschi Tags: Special Issue Article Source Type: research
Molecular design and synthesis of novel peptides from amphibians skin acting as inhibitors of cholinesterase enzymes
Cholinesterases are a family of enzymes that catalyze the hydrolysis of neurotransmitter acetylcholine. There are two types of cholinesterases, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), which differ in their distribution in the body. Currently, cholinesterase inhibitors (ChEI) represent the treatment of choice for Alzheimer's disease (AD). In this paper, we report the synthesis and inhibitory effect on both enzymes of four new peptides structurally related to P1‐Hp‐1971 (amphibian skin peptide found in our previous work. Sequence: TKPTLLGLPLGAGPAAGPGKR‐NH2). The bioassay data and cytotoxicity test...
Source: Journal of Peptide Science - February 1, 2017 Category: Biochemistry Authors: Alvaro Siano, Francisco F. Garibotto, Sebastian A. Andujar, Hector A. Baldoni, Georgina G. Tonarelli, Ricardo D. Enriz Tags: Research Article Source Type: research
Identification of laminin α5 short arm peptides active for endothelial cell attachment and tube formation
In this study, we identified active sequences for human umbilical vein endothelial cells (HUVECs) using recombinant proteins and synthetic peptides. The short arm of the α5 chain contains three globular domains [laminin N‐terminal globular domain, laminin 4 domain a, and laminin 4 domain b (LN, L4a, and L4b)] and three rod‐like elements [laminin epidermal growth factor‐like domain a, b, and c (LEa, LEb, and LEc)]. The cell attachment assay using recombinant proteins showed that RGD‐independent cell attachment sites were localized in the α5LN‐LEa domain. Further, we synthesized 70 peptides covering the amino aci...
Source: Journal of Peptide Science - January 31, 2017 Category: Biochemistry Authors: Yamato Kikkawa, Yumika Sugawara, Nozomi Harashima, Shogo Fujii, Kazuki Ikari, Jun Kumai, Fumihiko Katagiri, Kentaro Hozumi, Motoyoshi Nomizu Tags: Special Issue Article Source Type: research
Synthesis of ubiquitylated histone H3 using a thiirane linker for chemical ligation
In this report, we describe the preparation of the ubiquitylated full length histone H3 at the 18 position and the construction of tetranucleosomes with recombinant histones H2A, H2B, H4, and DNA, which are slightly more stable than those that are prepared without ubiquitin modification. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
Histone H3, ubiquitylated at the 18 position, was prepared by using a thiirane linker, which introduced a 1,2‐aminothiol moiety at the cysteine residue for native chemical ligation. The resulting isopeptide mimetic structure that was produced had the ability to f...
Source: Journal of Peptide Science - January 30, 2017 Category: Biochemistry Authors: Toru Kawakami, Yuichi Mishima, Hironobu Hojo, Isao Suetake Tags: Special Issue Article Source Type: research
Evaluation of combined use of Oxyma and HATU in aggregating peptide sequences
Polypeptides are finding increasing applications as therapeutics because of their specificity that often translates into excellent safety, tolerability, and efficacy profiles in humans. New synthetic methodologies for their preparation are thereby continuously sought to reduce the costs associated to chain assembly and purification. Although solid‐phase peptide synthesis has become one of the most advanced synthetic procedures at both laboratory and industrial scale, the process is often complicated by aggregation phenomena originating from the combined occurrence of intermolecular and intramolecular hydrogen bonding, hy...
Source: Journal of Peptide Science - January 30, 2017 Category: Biochemistry Authors: Andrea Caporale, Nunzianna Doti, Annamaria Sandomenico, Menotti Ruvo Tags: Special Issue Article Source Type: research
PepMat 2016: the second conference on peptide ‐based materials for biomedicine and nanotechnology
(Source: Journal of Peptide Science)
Source: Journal of Peptide Science - January 29, 2017 Category: Biochemistry Authors: Carlos Alem án, Ian W. Hamley, Meital Reches Tags: Editorial Source Type: research
Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides
The rise of CuI‐catalyzed click chemistry has initiated an increased demand for azido and alkyne derivatives of amino acid as precursors for the synthesis of clicked peptides. However, the use of azido and alkyne amino acids in peptide chemistry is complicated by their high cost. For this reason, we investigated the possibility of the in‐house preparation of a set of five Fmoc azido amino acids: β‐azido l‐alanine and d‐alanine, γ‐azido l‐homoalanine, δ‐azido l‐ornithine and ω‐azido l‐lysine. We investigated several reaction pathways described in the literature, suggested several improvements and p...
Source: Journal of Peptide Science - January 24, 2017 Category: Biochemistry Authors: Jan P ícha, Miloš Buděšínský, Kateřina Macháčková, Michaela Collinsová, Jiří Jiráček Tags: Research Article Source Type: research
