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Solvent environment conducive to protein aggregation
Author(s) -
Fernández Ariel,
de las Mercedes Boland Maria
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03392-6
Subject(s) - fibrillogenesis , chemistry , solvent , molecular dynamics , protein aggregation , protein folding , biophysics , folding (dsp implementation) , structuring , in vivo , computational chemistry , biochemistry , fibril , biology , finance , electrical engineering , economics , engineering , microbiology and biotechnology
The effect of solvent structuring induced by molecular crowding is elucidated within a competitive situation involving protein folding and aggregation. Two patterned fragments of amyloidogenic proteins are chosen as study cases and analyzed by molecular dynamics with an implicit treatment of the solvent. The extent of crowding needed to induce aggregation is determined. The results constitute a first step to assess the relevance of in vivo environments in understanding fibrillogenesis. The approach is independently validated by satisfactorily reproducing the results of an all‐atom explicit solvent trajectory.