The Role of HIV-1 gp41 Glycoprotein in Infectious Tropism Inferred from Physico-Chemical Properties of its Amino Acid Sequence

2006 ◽  
Author(s):  
E. Figueroa ◽  
C. Villarreal ◽  
L. Huerta ◽  
G. Cocho
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chemical Properties ◽  
Physico Chemical ◽  
Hiv 1

scholarly journals Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins

Crystals ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 1032
Author(s):  
Sonia Khemaissa ◽  
Sandrine Sagan ◽  
Astrid Walrant
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Hydrogen Bonds ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Noncovalent Interactions ◽  
Chemical Properties ◽  
Protein Stabilization ◽  
Physico Chemical

Tryptophan is an aromatic amino acid with unique physico-chemical properties. It is often encountered in membrane proteins, especially at the level of the water/bilayer interface. It plays a role in membrane protein stabilization, anchoring and orientation in lipid bilayers. It has a hydrophobic character but can also engage in many types of interactions, such as π–cation or hydrogen bonds. In this review, we give an overview of the role of tryptophan in membrane proteins and a more detailed description of the underlying noncovalent interactions it can engage in with membrane partners.

scholarly journals Specificity of the HIV-1 Protease on Substrates Representing the Cleavage Site in the Proximal Zinc-Finger of HIV-1 Nucleocapsid Protein

Viruses ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 1092
Author(s):  
János András Mótyán ◽  
Márió Miczi ◽  
Stephen Oroszlan ◽  
József Tőzsér
Keyword(s):  
Amino Acid ◽  
Zinc Finger ◽  
Cleavage Site ◽  
Potential Role ◽  
Binding Mode ◽  
Interaction Energies ◽  
Vitro Assay ◽  
Hiv 1

To explore the sequence context-dependent nature of the human immunodeficiency virus type 1 (HIV-1) protease’s specificity and to provide a rationale for viral mutagenesis to study the potential role of the nucleocapsid (NC) processing in HIV-1 replication, synthetic oligopeptide substrates representing the wild-type and modified versions of the proximal cleavage site of HIV-1 NC were assayed as substrates of the HIV-1 protease (PR). The S1′ substrate binding site of HIV-1 PR was studied by an in vitro assay using KIVKCF↓NCGK decapeptides having amino acid substitutions of N17 residue of the cleavage site of the first zinc-finger domain, and in silico calculations were also performed to investigate amino acid preferences of S1′ site. Second site substitutions have also been designed to produce “revertant” substrates and convert a non-hydrolysable sequence (having glycine in place of N17) to a substrate. The specificity constants obtained for peptides containing non-charged P1′ substitutions correlated well with the residue volume, while the correlation with the calculated interaction energies showed the importance of hydrophobicity: interaction energies with polar residues were related to substantially lower specificity constants. Cleavable “revertants” showed one residue shift of cleavage position due to an alternative productive binding mode, and surprisingly, a double cleavage of a substrate was also observed. The results revealed the importance of alternative binding possibilities of substrates into the HIV-1 PR. The introduction of the “revertant” mutations into infectious virus clones may provide further insights into the potential role of NC processing in the early phase of the viral life-cycle.

scholarly journals Occurrence of drug target residues within decantation tank sediments: a good clue to assess their historical excretion?

2021 ◽  
Vol 31 (1) ◽  
Author(s):  
Thomas Thiebault ◽  
Laëtitia Fougère ◽  
Anaëlle Simonneau ◽  
Emilie Destandau ◽  
Claude Le Milbeau ◽  
...  
Keyword(s):  
Drug Target ◽  
Chemical Properties ◽  
Deposition Process ◽  
Drug Consumption ◽  
Organic Layers ◽  
Sewer Systems ◽  
Physico Chemical ◽  
Deep Underground ◽  
Deposition Processes

AbstractThis study investigated the potential of sediments accumulated in sewer systems to record human activities through the occurrence of drug target residues (DTR). The installation studied is 17 m deep underground decantation tank that traps the coarse fractions of a unitary sewer system (northern part of Orléans, France), collecting both stormwater and wastewater. The sediments deposited in this tank could constitute a nonesuch opportunity to study the historical evolution of illicit and licit drug consumption in the catchment, however, the deposition processes and the record of DTRs remain largely unknown at present. Five cores were acquired from 2015 to 2017. One hundred fifty-two sediment samples were extracted using a mixture of ultra-pure water:methanol (1:1) prior to analysis of the extracts by high-pressure liquid chromatography coupled to tandem mass spectrometry. Several classical sedimentological analyses such as total organic carbon, facies description and granulometry were also performed on these samples, in order to understand the most important factors (e.g., physico-chemical properties of the DTRs, solid type, assumed load in wastewater) impacting their deposition.The key role of the speciation of DTRs was highlighted by the higher contents in neutral and anionic DTRs in organic layers, whereas only cationic DTRs were found in mineral layers. The considerable modifications in the sediments’ properties, generated by distinct origins (i.e., stormwater or wastewater), are therefore the most important drivers that must be taken into account when back-calculating the historical patterns of drug consumption from their DTR concentrations in decantation tank sediments. Further research remains necessary to fully understand the deposition process, but this study provides new clues explaining these temporal evolutions.

Amino acid composition and physico-chemical properties of bluefin tuna (Thunnus thynnus) myoglobin

1978 ◽  
Vol 60 (2) ◽  
pp. 195-199 ◽  
Author(s):  
Ciro Balestrieri ◽  
Giovanni Colonna ◽  
Alfonso Giovane ◽  
Gaetano Irace ◽  
Luigi Servillo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chemical Properties ◽  
Bluefin Tuna ◽  
Thunnus Thynnus ◽  
Physico Chemical

scholarly journals Impact of Quantum Dot Surface on Complex Formation with Chlorin e6 and Photodynamic Therapy

Nanomaterials ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 9 ◽  
Author(s):  
Artiom Skripka ◽  
Dominyka Dapkute ◽  
Jurga Valanciunaite ◽  
Vitalijus Karabanovas ◽  
Ricardas Rotomskis
Keyword(s):  
Photodynamic Therapy ◽  
Cancer Therapy ◽  
Complex Formation ◽  
Chemical Properties ◽  
Disease Diagnosis ◽  
Chlorin E6 ◽  
Deep Tissue ◽  
Physico Chemical

Nanomaterials have permeated various fields of scientific research, including that of biomedicine, as alternatives for disease diagnosis and therapy. Among different structures, quantum dots (QDs) have distinctive physico-chemical properties sought after in cancer research and eradication. Within the context of cancer therapy, QDs serve the role of transporters and energy donors to photodynamic therapy (PDT) drugs, extending the applicability and efficiency of classic PDT. In contrast to conventional PDT agents, QDs’ surface can be designed to promote cellular targeting and internalization, while their spectral properties enable better light harvesting and deep-tissue use. Here, we investigate the possibility of complex formation between different amphiphilic coating bearing QDs and photosensitizer chlorin e6 (Ce6). We show that complex formation dynamics are dependent on the type of coating—phospholipids or amphiphilic polymers—as well as on the surface charge of QDs. Förster’s resonant energy transfer occurred in every complex studied, confirming the possibility of indirect Ce6 excitation. Nonetheless, in vitro PDT activity was restricted only to negative charge bearing QD-Ce6 complexes, correlating with better accumulation in cancer cells. Overall, these findings help to better design such and similar complexes, as gained insights can be straightforwardly translated to other types of nanostructures—expanding the palette of possible therapeutic agents for cancer therapy.

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