Effect of low molecular weight aliphatic alcohols and related compounds on platelet factor 4 subunit association

Yang, Yisong; Barker, Sharon; Chen, Mu Jung; Mayo, Kevin H.

doi:10.1016/s0021-9258(18)98339-0

Cited by 27 publications

(12 citation statements)

References 21 publications

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“…Protein concentration was determined by using the bicinchoninic acid assay [27]. [19,20]. The final protein concentration was 18 mg\ml.…”

Section: Isolation Of Recombinant Nap-2mentioning

confidence: 99%

“…Monomeric NAP-2 was generated by adding to the solution 4 % (v\v) 2-chloroethanol, which is known to dissociate the dimeric and tetrameric aggregation states of the protein [19,20]. Because "H-NMR sequence-specific assignments for monomeric NAP-2 are known [19], heteronuclear "H-"&N 2D-NMR and 3D-NMR experiments were performed to acquire "&N resonance assignments and additional NOE distance constraints and motional dynamics information.…”

Section: Resonance Assignmentsmentioning

confidence: 99%

“…In previous NMR studies of NAP-2 [13,19], the selfassociation-induced exchange broadening of resonances and the presence of multiple aggregate states were overcome by using various agents (salts and organic compounds) to disaggregate NAP-2. The most effective of these is 2-chloroethanol [20], which at low concentration [3-4 % (v\v)] essentially dissociates NAP-2 to the monomeric state [19]. This allowed most "H sequencespecific assignments to be made for monomeric NAP-2 and secondary structural elements to be deduced from a qualitative interpretation of "H nuclear Overhauser effects (NOEs), $J α N coupling constants and long-lived backbone NH groups [19].…”

Section: Introductionmentioning

confidence: 99%

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NMR structure and dynamics of monomeric neutrophil-activating peptide 2

Young

Roongta

Daly

et al. 1999

Biochemical Journal

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Neutrophil-activating peptide 2 (NAP-2), which demonstrates a range of proinflammatory activities, is a 72-residue protein belonging to the alpha-chemokine family. Although NAP-2, like other alpha-chemokines, is known to self-associate into dimers and tetramers, it has been shown that the monomeric form is physiologically active. Here we investigate the solution structure of monomeric NAP-2 by multi-dimensional 1H-NMR and 15N-NMR spectroscopy and computational modelling. The NAP-2 monomer consists of an amphipathic, triple-stranded, anti-parallel beta-sheet on which is folded a C-terminal alpha-helix and an aperiodic N-terminal segment. The backbone fold is essentially the same as that found in other alpha-chemokines. 15N T1, T2 and nuclear Overhauser effects (NOEs) have been measured for backbone NH groups and used in a model free approach to calculate order parameters and conformational exchange terms that map out motions of the backbone. N-terminal residues 1 to 17 and the C-terminus are relatively highly flexible, whereas the beta-sheet domain forms the most motionally restricted part of the fold. Conformational exchange occurring on the millisecond time scale is noted at the top of the C-terminal helix and at proximal residues from beta-strands 1 and 2 and the connecting loop. Dissociation to the monomeric state is apparently responsible for increased internal mobility in NAP-2 compared with dimeric and tetrameric states in other alpha-chemokines.

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“…Protein concentration was determined by using the bicinchoninic acid assay [27]. [19,20]. The final protein concentration was 18 mg\ml.…”

Section: Isolation Of Recombinant Nap-2mentioning

confidence: 99%

Section: Resonance Assignmentsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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NMR structure and dynamics of monomeric neutrophil-activating peptide 2

Young

Roongta

Daly

et al. 1999

Biochemical Journal

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“…4,5 Although TFE can stabilize other secondary structure motifs, 6,7 its total effect on the tertiary structure of nonhelical proteins tends to be rather denaturing. 4,8 TFE can often destabilize even the quaternary structure of proteins, 9,10 and it was also reported that TFE is able to promote aggregation. 11 In contrast, addition of TFE was found to be necessary for maintaining the fold of an artificial miniprotein.…”

Section: ■ Introductionmentioning

confidence: 98%

Effect of TFE on the Helical Content of AK17 and HAL-1 Peptides: Theoretical Insights into the Mechanism of Helix Stabilization

2016

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Fluorinated alcohols such as 2,2,2-trifluoroethanol (TFE) are among the most frequently used cosolvents in experiment studies of peptides. They have significant effects on secondary structure and a particularly strong promotion of α-helix is induced by TFE. In this study we validated recently proposed force field parameters for TFE in molecular dynamics simulations with two model peptides-alanine-rich AK-17 and antimicrobial peptide halictine-1 (HAL-1). In the case of HAL-1, we characterized the effect of TFE on this peptide experimentally by ECD spectroscopy. Our TFE model in question reproduced the helix-promoting effect of TFE and provided insight into the mechanisms of TFE action on peptides. Our simulations confirmed the preferential interaction of TFE molecules with α-helices, although the TFE molecules accumulate in the vicinity of the peptides in various conformations. Moreover, we observed a significant effect of TFE on the thermodynamics of the helix-coil transition and a change in local conformational preferences in the unfolded (coil) state induced by TFE. In addition, our simulation-based analysis suggests that different mechanisms participate in helix stabilization in both model peptides in water and TFE solution. Our results thus support the picture of complex TFE action on peptides that is further diversified by the identity and intrinsic properties of the peptide.

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“…Moreover, in inflamed tissues, local concentrations can be much greater, with their homodimeric state being significantly influenced by the overall cellular environment, e.g. local pH, binding partners, ligands, and hydrophobic vs. hydrophilic interactions, as exemplified with CXCL4 (PF4) under various solution conditions [ 75 ]. Therefore, dissociation constants for chemokine dimerization measured in vitro are likely to be higher than those from a given chemokine in a physiological environment [ 69 ].…”

Section: Chemokine Structuresmentioning

confidence: 99%

The marriage of chemokines and galectins as functional heterodimers

Hundelshausen

Wichapong

Gabius

et al. 2021

Cell. Mol. Life Sci.

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Trafficking of leukocytes and their local activity profile are of pivotal importance for many (patho)physiological processes. Fittingly, microenvironments are complex by nature, with multiple mediators originating from diverse cell types and playing roles in an intimately regulated manner. To dissect aspects of this complexity, effectors are initially identified and structurally characterized, thus prompting familial classification and establishing foci of research activity. In this regard, chemokines present themselves as role models to illustrate the diversification and fine-tuning of inflammatory processes. This in turn discloses the interplay among chemokines, their cell receptors and cognate glycosaminoglycans, as well as their capacity to engage in new molecular interactions that form hetero-oligomers between themselves and other classes of effector molecules. The growing realization of versatility of adhesion/growth-regulatory galectins that bind to glycans and proteins and their presence at sites of inflammation led to testing the hypothesis that chemokines and galectins can interact with each other by protein–protein interactions. In this review, we present some background on chemokines and galectins, as well as experimental validation of this chemokine–galectin heterodimer concept exemplified with CXCL12 and galectin-3 as proof-of-principle, as well as sketch out some emerging perspectives in this arena.

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Effect of low molecular weight aliphatic alcohols and related compounds on platelet factor 4 subunit association

Cited by 27 publications

References 21 publications

NMR structure and dynamics of monomeric neutrophil-activating peptide 2

NMR structure and dynamics of monomeric neutrophil-activating peptide 2

Effect of TFE on the Helical Content of AK17 and HAL-1 Peptides: Theoretical Insights into the Mechanism of Helix Stabilization

The marriage of chemokines and galectins as functional heterodimers

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