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Human Eosinophil Lysophospholipase (Charcot-Leyden Crystal Protein): Molecular Cloning, Expression, and Potential Functions in Asthma
Published in Gerald J. Gleich, A. Barry Kay, Eosinophils in Allergy and Inflammation, 2019
Steven J. Ackerman, Zeqi Zhou, Daniel G. Tenen, Mike A. Clark, Yuan-Po Tu, Charles G. Irvin
The 426-bp open reading frame encoded a 142-amino-acid polypeptide with a predicted mass of 16.5 kDa, isoelectric point of 7.28, and a single potential N-linked glycosylation site (Asn-Val-Ser) (56) at amino acids 136–138. Comparisons of the predicted amino acid composition from the CLC cDNA clone with that of authentic CLC protein (10) and eosinophil lysophospholipase (13) showed them to be essentially identical (Table 1). Hydrophobic (A, I, L, W, V) and aromatic (F, Y) residues comprise 36.6% of the amino acids, and there are equivalent numbers of strongly basic (K, R) and strongly acidic (D, E) residues. In contrast to the marked number of hydrophobic and aromatic residues, a Kyte and Doolittle (57) hydrophobicity profile showed relatively few markedly hydrophobic domains in the sequence aside from a hydrophobic amino terminus of seven residues that does not appear to resemble a typical cleaved (58) or uncleaved signal sequence (59,60) and hydrophobic regions containing the two cysteine residues in the sequence one of which contributes the reactive thiol group thought to comprise part of the active site of this sulfhydryl-dependent lysophospholipase (13). Secondary structure as evaluated by the method of Chou and Fassman (61) suggests 37% helical, 80% extended, and 21% beta-turn conformations.
Immunodominant regions prediction of nucleocapsid protein for SARS-CoV-2 early diagnosis: a bioinformatics and immunoinformatics study
Published in Pathogens and Global Health, 2020
Yufeng Dai, Hongzhi Chen, Siqi Zhuang, Xiaojing Feng, Yiyuan Fang, Haoneng Tang, Ruchun Dai, Lingli Tang, Jun Liu, Tianmin Ma, Guangming Zhong
Considering that structures such as beta-turn and random coil are more conducive to bind with the specific B cell receptor (BCR), we adopted SOPMA online software to predict the secondary structure of N protein (Figure S2C). To ensure the structural integrity of the predicted epitopes, we adjusted the terminus of the selected regions by appropriately adding several amino acid residues at both ends. By synthesizing the results of hydrophilicity, surface accessibility, and secondary structure analysis, we altered N164-221 to N161-221; N361-399 to N354-399. Hereinabove, N1-51, N161-221, N229-269, N354-399, and N408-416 were selected, which contained several potential B-cell epitopes with a high antigenicity score.
N-Methyl-D-Aspartate (NMDA) receptor modulators: a patent review (2015-present)
Published in Expert Opinion on Therapeutic Patents, 2020
Hazem Ahmed, Ahmed Haider, Simon M. Ametamey
Northwestern University filed a patent claiming a peptidomimetic class of NMDA receptor modulators [148]. These peptidomimetics adopt a beta-turn motif when bound to the glycine binding site. [3H]TCP was the radioligand of choice for binding affinity determination of the target compounds, while GLYX-13 was used as a comparator in in vitro biological experiments. The tested compounds proved to be more potent than GLYX-13 in LTP, however, GLYX-13 concurrently increased LTP and reduced long-term depression (LTD). These results were supplemented by in vivo experiments including memory and learning enhancement amongst others. Spirolactams were a major subset of the compounds discussed in this patent. Indeed, spirolactams have been covered by several patents as NMDA receptor modulators by Naurex and Aptinyx, and three compounds (NYX-458, NYX-783, and NYX-2925) are currently reported to be in clinical trials (ClinicalTrials.gov Identifier: NCT04148391, NCT04044664, and NCT04147858) for the treatment of mild cognitive impairment that is associated with Parkinson’s disease, post-traumatic stress disorder, neuropathic pain associated with diabetic peripheral neuropathy and fibromyalgia [149–154].
An overview of the recent progress in Middle East Respiratory Syndrome Coronavirus (MERS-CoV) drug discovery
Published in Expert Opinion on Drug Discovery, 2023
In addition to the spike, nucleocapsid, envelope, and matrix proteins and the helicase enzyme, the MERS-CoV RNA genome also encodes an RNA-dependent RNA polymerase (RdRp) [17]. The polymerase’s RdRp domain has a conserved fold that is defined by two successive aspartates protruding from a beta-turn structure [101]. Several studies showed that inhibiting viral polymerases is effective in preventing SARS-CoV infections. Therefore, it would be reasonable to investigate the consequences of inhibiting RdRp in MERS-CoV [102].