New insights into side effect of solvents on the aggregation of human islet amyloid polypeptide 11–20

Mao, Yexuan; Yu, Lanlan; Yang, Ran; Ma, Cheng; Qu, Lingbo; Harrington, Peter de B.

doi:10.1016/j.talanta.2015.11.012

Cited by 17 publications

(16 citation statements)

References 29 publications

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“…However, the buffer may play a critical role in protein aggregations. Yexuan Mao et al [27] reported the effect of solvents on the aggregation of human islet amyloid polypeptides [11][12][13][14][15][16][17][18][19][20]. They found different behaviors of the peptides aggregation under different buffering systems.…”

Section: Solvent and Concentration Range Considerationsmentioning

confidence: 99%

“…On the other hand, biochemical and biophysical techniques are attractive and developed dramatically to be the first choice in studying biomolecular interactions. Examples include spectroscopic techniques [13][14][15][16][17][18], surface plasma resonance (SPR) [19][20][21], isothermal titration calorimetry (ITC) [22][23][24] and microscale thermophoresis (MST) [25][26][27]. This review will discuss thermophoresis in the characterization of biomolecular interactions.…”

Section: Introductionmentioning

confidence: 99%

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Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

101

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The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

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Section: Solvent and Concentration Range Considerationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

101

View full text Add to dashboard Cite

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“…Our previous study has reported that hIAPP 11‐20 is a peptide with great tendency to self‐aggregate in aqueous solution and the binding affinity of hIAPP 11‐20 self‐aggregation was achieved with the dissociation constant K d of 6.64 μmol L −1 . The ThT fluorescence measurements demonstrated that lipopeptides with long‐chain alkane have extraordinary inhibitory effect on hIAPP 11‐20 amyloid formation, and therefore, these lipopeptides with high inhibitory effect were chosen for binding affinity investigation.…”

Section: Resultsmentioning

confidence: 99%

“…Microscale thermophoresis is a useful tool to be applied in calculating the parameters of ΔH and ΔS through measuring the affinities of the same sample at various temperatures. [34] Typically, many types of forces exist in molecular interaction, such as hydrogen bonding, van der Waals force, electrostatic and hydrophobic interactions. Ross and The aggregation morphology of human islet amyloid polypeptide residues 11-20 alone at A, 0 and B, 24 h; human islet amyloid polypeptide residues 11-20 was incubated in the presence of C14R4 with the molar ratio of 1:1 at C, 0 and D, 48 h. Incubation temperature was fixed at 37°C…”

Section: Thermodynamic Parameters By Mstmentioning

confidence: 99%

Design and study of lipopeptide inhibitors on preventing aggregation of human islet amyloid polypeptide residues 11‐20

Mao

et al. 2017

Journal of Peptide Science

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Type 2 diabetes mellitus, a kind of conformational disease, has become an epidemic disease, which seriously endangers the quality of life and health of human beings. The deposition of human islet amyloid polypeptide (hIAPP) has been considered as one of the major pathological features of type 2 diabetes mellitus. As lipopeptides have some hydrophobic groups, which are similar to the reported aggregation inhibitors, and some lipopeptides could prevent cells from depositing of amyloid fibrils, several potential lipopeptide inhibitors have been engineered and synthesized, which have been assessed for their inhibitory effect in preventing amyloid fibrils formation of hIAPP [11][12][13][14][15][16][17][18][19][20] by using the conventional thioflavin-T fluorescence assay and new technique microscale thermophoresis (MST). The final amyloid fibrils of hIAPP [11][12][13][14][15][16][17][18][19][20] were characterized by transmission electron microscopy. Results suggested that with the increasing length of alkyl chain, the antiaggregation efficiency of lipopeptide inhibitors towards hIAPP 11-20 increased gradually.Meanwhile, the amount of arginines, which represent the head groups of lipopeptides, may also have some influence. The binding events also showed that the inhibitory efficiency of these lipopeptide inhibitors was enhanced with the increase of affinities between lipopeptides and hIAPP [11][12][13][14][15][16][17][18][19][20] , which were obtained from MST. This study demonstrated the efficiency of lipopeptides in inhibiting the aggregation of hIAPP [11][12][13][14][15][16][17][18][19][20] and proved that MST could be regarded as an appropriate and rapid method to screen potential inhibitors of hIAPP [11][12][13][14][15][16][17][18][19][20] or other amyloid proteins. This study also broadens the types of inhibitors on inhibiting amyloid formation of hIAPP.

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“…The Kd for PVP10 binding to IAPP was found to be 1.14±0.54 M. Therefore, PVP10 interacts strongly with IAPP monomers, with a Kd smaller than that of self-aggregating IAPP11-20 in PBS (6.56 M) [58]. This suggests that PVP10 may inhibit IAPP assembly by weakening the interaction of IAPP with itself, resulting in reduced self-aggregation.…”

Section: Pvp10-iapp Interaction Kd Determinationmentioning

confidence: 96%

Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition

Berwick

Vaux

Jean

2018

Biochemical Journal

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Deposition of misfolded amyloid polypeptides, associated with cell death, is the hallmark of many degenerative diseases (e.g. type II diabetes mellitus and Alzheimer's disease). In vivo, cellular and extracellular spaces are occupied by a high volume fraction of macromolecules. The resulting macromolecular crowding energetically affects reactions. Amyloidogenesis can either be promoted by macromolecular crowding through the excluded volume effect or inhibited due to a viscosity increase reducing kinetics. Macromolecular crowding can be mimicked in vitro by the addition of non-specific polymers, e.g. Ficoll, dextran and polyvinyl pyrrolidone (PVP), the latter being rarely used to study amyloid systems. We investigated the effect of PVP on amyloidogenesis of full-length human islet amyloid polypeptide (involved in type II diabetes) using fibrillisation and surface activity assays, ELISA, immunoblot and microscale thermophoresis. We demonstrate that high molecular mass PVP360 promotes amyloidogenesis due to volume exclusion and increase in effective amyloidogenic monomer concentration, like other crowders, but without the confounding effects of viscosity and surface activity. Interestingly, we also show that low molecular mass PVP10 has unique inhibitory properties as inhibition of fibril elongation occurs mainly in the bulk solution and is due to PVP10 directly and strongly interacting with amyloid species rather than the increase in viscosity typically associated with macromolecular crowding. In vivo, amyloidogenesis might be affected by the properties and proximity of endogenous macromolecular crowders, which could contribute to changes in associated pathogenesis. More generally, the PVP10 molecular backbone could be used to design small compounds as potential inhibitors of toxic species formation.

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New insights into side effect of solvents on the aggregation of human islet amyloid polypeptide 11–20

Cited by 17 publications

References 29 publications

Thermophoresis for characterizing biomolecular interaction

Thermophoresis for characterizing biomolecular interaction

Design and study of lipopeptide inhibitors on preventing aggregation of human islet amyloid polypeptide residues 11‐20

Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition

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