Spatial Structures of PAP(262–270) and PAP(274–284), Two Selected Fragments of PAP(248–286), an Enhancer of HIV Infectivity

Blokhin, Dmitriy; Филиппов, А. В.; Antzutkin, Oleg N.; Afonin, Sergii; Клочков, В. В.

doi:10.1007/s00723-015-0669-0

Cited by 8 publications

(5 citation statements)

References 18 publications

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“…In addition, the nuclear Overhauser effect experiment in a rotating system of coordinates (1H–1H 2D ROESY) was carried out to confirm of the space orientation of L2 to oxygen atoms of Co(III)P2. Recently, this method has been successfully applied to define the spatial structure of macromolecules [ 36 , 37 , 38 , 39 ], and the small biologically active molecules [ 40 ]. This experiment unambiguously showed through space interactions of ligand protons with the Co(III)P protons located in close proximity to oxygen.…”

Section: Results and Its Discussionmentioning

confidence: 99%

Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrins in Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions

et al. 2021

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Bymeans of spectrophotometric titration and NMR spectroscopy, the selective binding ability ofthe Co(III)-5,15-bis-(3-hydroxyphenyl)-10,20-bis-(4-sulfophenyl)porphyrin (Со(III)Р1) andCo(III)-5,15-bis-(2-hydroxyphenyl)-10,20-bis-(4-sulfophenyl)porphyrin (Со(III)Р2) towards imidazole derivatives of various nature (imidazole (L1), metronidazole (L2), and histamine (L3)) in phosphate buffer (pH 7.4) has been studied. It was found that in the case of L2, L3 the binding of the “first” ligand molecule by porphyrinatesCo(III)P1 and Co(III)P2 occurs with the formation of complexes with two binding sites (donor–acceptor bond at the center and hydrogen bond at the periphery of the macrocycle), while the “second” ligand molecule is added to the metalloporphyrin only due to the formation of the donor–acceptor bond at the macrocycle coordination center. The formation of stable complexes with two binding sites has been confirmed by density functional theory method (DFT) quantum chemical calculations and two-dimensional NMR experiments. It was shown that among the studied porphyrinates, Co(III)P2 is more selective towards to L1-L3 ligands, and localization of cobalt porphyrinates in cetylpyridinium chloride (CPC) micelles does not prevent the studied imidazole derivatives reversible binding. The obtained materials can be used to develop effective receptors for recognition, delivery, and prolonged release of drug compounds to the sites of their functioning. Considering that cetylpyridinium chloride is a widely used cationic biocide as a disinfectant, the designed materials may also prove to be effective antimicrobial agents.

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Section: Results and Its Discussionmentioning

confidence: 99%

Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrins in Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions

et al. 2021

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“…It can be noted that SEM1(45-67) contains helix (E58-K60) and an ordered helix-like structure (S49-Q51) in comparison to SEM1 (49)(50)(51)(52)(53)(54)(55)(56)(57)(58)(59)(60)(61)(62)(63)(64)(65)(66)(67). In previous articles, the constant secondary structure was observed for individual peptide fragments (PAP(248-261), PAP(262-270) and PAP(274-284)) [43,44], as well as a part of a full-sized PAP(248-286) peptide [45]. Based on the assumption of the secondary structure conservation of individual peptides as well as full-sized protein, the presence of helical fragment SEM1 in the SEM1(45-107) spatial structure was supposed.…”

Section: Discussionmentioning

confidence: 98%

Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation

Osetrina,

Kusova,

Bikmullin

et al. 2023

IJMS

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It is known that four peptide fragments of predominant protein in human semen Semenogelin 1 (SEM1) (SEM1(86–107), SEM1(68–107), SEM1(49–107) and SEM1(45–107)) are involved in fertilization and amyloid formation processes. In this work, the structure and dynamic behavior of SEM1(45–107) and SEM1(49–107) peptides and their N-domains were described. According to ThT fluorescence spectroscopy data, it was shown that the amyloid formation of SEM1(45–107) starts immediately after purification, which is not observed for SEM1(49–107). Seeing that the peptide amino acid sequence of SEM1(45–107) differs from SEM1(49–107) only by the presence of four additional amino acid residues in the N domain, these domains of both peptides were obtained via solid-phase synthesis and the difference in their dynamics and structure was investigated. SEM1(45–67) and SEM1(49–67) showed no principal difference in dynamic behavior in water solution. Furthermore, we obtained mostly disordered structures of SEM1(45–67) and SEM1(49–67). However, SEM1(45–67) contains a helix (E58-K60) and helix-like (S49-Q51) fragments. These helical fragments may rearrange into β-strands during amyloid formation process. Thus, the difference in full-length peptides’ (SEM1(45–107) and SEM1(49–107)) amyloid-forming behavior may be explained by the presence of a structured helix at the SEM1(45–107) N-terminus, which contributes to an increased rate of amyloid formation.

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“…Freshly synthesized PAP(248–286) did not enhance HIV infection, while agitation of PAP(248–286) led to amyloid fibril formation. Highly cationic SEVI fibrils (pI of 10.21) enhance HIV infection in a charge-dependent manner by reducing the electrostatic repulsion between the cell surface and the HIV virion, as well as by binding to virions and increasing their deposition on the cell surface. − SEVI fibrils have been shown to have a clear unbranched fibrillar structure, identical to other known amyloid fibrils. − Amyloids promote nucleation-dependent elongation mechanisms, specifically thioflavin T (ThT) binding, indicating the presence of a cross-β structure. − …”

Section: Introductionmentioning

confidence: 99%

PAP(248–286) Conformational Changes during the Lag Phase of Amyloid Fibril Formation

2023

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The initial stage of fibril formation of C-terminal region PAP(248–286) of human seminal plasma protein prostatic acid phosphatase was considered. Amyloid fibrils from the peptide PAP(248–286) are termed as a semen-derived enhancer of viral infection (SEVI) found in abundant quantities in semen. The kinetics of the amyloid fibril formation process consists of two characteristic phases (lag phase/nucleation phase and growth phase/elongation phase). The lag phase can be caused by the presence of mature amyloid fibrils (seeds) in protein solution, so-called secondary nucleation. The secondary nucleation includes interaction of protein monomers with the mature fibril surface that leads to protein spatial structural changes for further amyloid fibril formation. In this work, changes of the PAP(248–286) spatial structure were obtained during the secondary nucleation phase. Pulsed-field gradient (PFG) NMR was used to characterize the behavior of monomeric PAP(248–286) in water solution after PAP(248–286) seed addition. The self-diffusion coefficient showed compactization of the peptide monomer due to fibril–monomer interactions. PAP(248–286) spatial structural changes were detected with the help of high-resolution NMR spectroscopy and molecular dynamics (MD) simulation. The folding of PAP(248–286) occurs due to backbone chain bending in the region of H270 and T275 amino acid residues. Obtained folded conformation of PAP(248–286) emerging in the secondary nucleation process is energetically favorable and retains after monomer–amyloid interaction. The structural changes are associated with localization of PAP(248–286) hydrophobic surface regions, which are probably responsible for peptide monomer–amyloid interactions.

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Spatial Structures of PAP(262–270) and PAP(274–284), Two Selected Fragments of PAP(248–286), an Enhancer of HIV Infectivity

Cited by 8 publications

References 18 publications

Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrins in Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions

Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrins in Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions

Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation

PAP(248–286) Conformational Changes during the Lag Phase of Amyloid Fibril Formation

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