期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 117, 期 6, 页码 1770-1779出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp306386p
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资金
- National Science Foundation [CHE-090974]
- Alexander von Humboldt Foundation
- Direct For Mathematical & Physical Scien [0909743] Funding Source: National Science Foundation
- Division Of Chemistry [0909743] Funding Source: National Science Foundation
We have probed the structures and aggregation propensities of chirally substituted [Ala(2)]-Leu-Enkephalin peptides (i.e., Leu-Enkephalin G2A) with a combination of ion-mobility spectrometry/mass spectrometry and techniques of computational chemistry. Our IMS/MS data reveal a strong correlation between the propensity to form peptide dimers and the subsequent aggregation propensity. This correlation indicates that the dimerization process is fundamental to the overall self-assembly process. Our computational data correlate a conformational conversion during the peptide association process with a reduced experimental dimer formation and subsequent aggregation propensity. Furthermore, our analysis indicates that monomer activation does not precede peptide association and thus suggests that the entire-refolding or gain-in-interaction models are more realistic accounts of the peptide self-assembly process than the monomer-conversion model. In sum, our results suggest that conformational transitions of early peptide oligomers represent bottlenecks of the peptide self-assembly process and thus highlight the importance of structurally characterizing this reaction during amyloid formation.
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