Dynamics and Rigidity in an Intrinsically Disordered Protein, β-Casein

Perticaroli, Stefania; Nickels, Jonathan D.; Ehlers, Georg; Mamontov, Eugene; Sokolov, Alexei P.

doi:10.1021/jp503788r

Cited by 48 publications

(68 citation statements)

References 63 publications

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“…Comparatively, crosslinked glycation structures including pentosidine, GOLD and MOLD can connect different protein chains together, thus limiting the flexibility of the protein chain and resulting in higher hindrance to the proteolysis . The hindrance of crosslinked glycation structure to proteolysis in this study was shown to be less significant in glycated β ‐CN, which could also be attributed to its intrinsic flexible and open structure …”

Section: Resultsmentioning

confidence: 66%

“…By contrast, the DH value of β ‐CN glycated with 10 mmol L −1 glucose did not show a significant decrease in either gastric or intestinal digestion. This finding may be related to the intrinsic disordered structure of β ‐CN . The flexible structure and high thermal stability of β ‐CN may weaken hindrance induced by glycation structures to the action of digestive proteases.…”

Section: Resultsmentioning

confidence: 98%

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Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

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BACKGROUND Milk proteins are widely used in food production and are often glycated by reducing sugar. Although many studies have reported the digestibility of glycated milk protein, most have focused on measuring degree of hydrolysis (DH), showing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) image of digests. Detailed information on the changes in peptide composition of digests has seldom been revealed. Therefore, in addition to measuring the DH and showing the SGS‐PAGE images of digests, we also analyzed the peptidomics in digests using liquid chromatography–electrospray ionization–tandem mass spectrometry (LC‐ESI‐MS/MS) and Mascot database in this work to further reveal the influence of glycation on protein nutrition. RESULTS Compared with β‐lactoglobulin and bovine serum albumin (BSA), DH of β‐casein was suppressed to a lesser extent by glycation in both gastric and intestinal stages. Aggregates of glycated BSA were less sensitive to the action of digestive enzymes throughout gastrointestinal digestion according to SDS‐PAGE images. Changes in the peptide composition of digests induced by glycation were distinctly displayed, showing both absence of peptides and occurrence of new peptides, based on the results obtained from LC‐ESI‐MS/MS. CONCLUSIONS Glycation can greatly change the peptide composition in digests of milk protein. The nutritional impact of the change in the peptide composition requires further investigation, and the impact of MRPs in unabsorbed digests on the gut flora should be an interesting field for further studies. © 2018 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 66%

Section: Resultsmentioning

confidence: 98%

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

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“…The side chain dynamics depend on the length and polarity of the amino acid residue, as well as on the chemical environment of the side chain, which in turn is determined by the folding of the entire protein chain. Accordingly, an unfolded polypeptide chain is more flexible than a tightly folded globular protein [50,51]. …”

Section: Resultsmentioning

confidence: 99%

Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering—A Comparison between Wild-Type Protein and a Hinge Mutant

et al. 2015

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Myelin protein P2 is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system, and its function is related to its membrane binding capacity. Here, the link between P2 protein dynamics and structure and function was studied using elastic incoherent neutron scattering (EINS). The P38G mutation, at the hinge between the β barrel and the α-helical lid, increased the lipid stacking capacity of human P2 in vitro, and the mutated protein was also functional in cultured cells. The P38G mutation did not change the overall structure of the protein. For a deeper insight into P2 structure-function relationships, information on protein dynamics in the 10 ps to 1 ns time scale was obtained using EINS. Values of mean square displacements mainly from protein H atoms were extracted for wild-type P2 and the P38G mutant and compared. Our results show that at physiological temperatures, the P38G mutant is more dynamic than the wild-type P2 protein, especially on a slow 1-ns time scale. Molecular dynamics simulations confirmed the enhanced dynamics of the mutant variant, especially within the portal region in the presence of bound fatty acid. The increased softness of the hinge mutant of human myelin P2 protein is likely related to an enhanced flexibility of the portal region of this fatty acid-binding protein, as well as to its interactions with the lipid bilayer surface requiring conformational adaptations.

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“…As before, we reduce the charge on nESI generated protein ions and examine the CCSDs of precursor and product ions. We compare the structural change when the charge is reduced for a rigid (BPTI) [48, 49] and for an intrinsically disordered protein (beta casein) [50–52]. …”

Section: Introductionmentioning

confidence: 99%

Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum

Jhingree

Bellina

Pacholarz

et al. 2017

J. Am. Soc. Mass Spectrom.

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Charge reduction in the gas phase provides a direct means of manipulating protein charge state, and when coupled to ion mobility mass spectrometry (IM-MS), it is possible to monitor the effect of charge on protein conformation in the absence of solution. Use of the electron transfer reagent 1,3-dicyanobenzene, coupled with IM-MS, allows us to monitor the effect of charge reduction on the conformation of two proteins deliberately chosen from opposite sides of the order to disorder continuum: bovine pancreatic trypsin inhibitor (BPTI) and beta casein. The ordered BPTI presents compact conformers for each of three charge states accompanied by narrow collision cross-section distributions (TWCCSDN2→He). Upon reduction of BPTI, irrespective of precursor charge state, the TWCCSN2→He decreases to a similar distribution as found for the nESI generated ion of identical charge. The behavior of beta casein upon charge reduction is more complex. It presents over a wide charge state range (9–28), and intermediate charge states (13–18) have broad TWCCSDN2→He with multiple conformations, where both compaction and rearrangement are seen. Further, we see that the TWCCSDN2→He of the latter charge states are even affected by the presence of radical anions. Overall, we conclude that the flexible nature of some proteins result in broad conformational distributions comprised of many families, even for single charge states, and the barrier between different states can be easily overcome by an alteration of the net charge. Graphical Abstractᅟ Electronic supplementary materialThe online version of this article (doi:10.1007/s13361-017-1692-1) contains supplementary material, which is available to authorized users.

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Dynamics and Rigidity in an Intrinsically Disordered Protein, β-Casein

Cited by 48 publications

References 63 publications

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering—A Comparison between Wild-Type Protein and a Hinge Mutant

Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum

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