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-Structure paper
タイトル | Atomic structures of naphthalene dipeptide micelles unravel mechanisms of assembly and gelation. |
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ジャーナル・号・ページ | Cell Rep Phys Sci, Vol. 5, Issue 2, Year 2024 |
掲載日 | 2024年2月21日 |
![]() | Ravi R Sonani / Simona Bianco / Bart Dietrich / James Doutch / Emily R Draper / Dave J Adams / Edward H Egelman / ![]() ![]() |
PubMed 要旨 | Peptide-based biopolymers have gained increasing attention due to their versatile applications. A naphthalene dipeptide (2NapFF) can form chirality-dependent tubular micelles, leading to ...Peptide-based biopolymers have gained increasing attention due to their versatile applications. A naphthalene dipeptide (2NapFF) can form chirality-dependent tubular micelles, leading to supramolecular gels. The precise molecular arrangement within these micelles and the mechanism governing gelation have remained enigmatic. We determined, at near-atomic resolution, cryoelectron microscopy structures of the 2NapFF micelles LL-tube and LD-tube, generated by the stereoisomers (l,l)-2NapFF and (l,d)-2NapFF, respectively. The structures reveal that the fundamental packing of dipeptides is driven by the systematic π-π stacking of aromatic rings and that same-charge repulsion between the carbonyl groups is responsible for the stiffness of both tubes. The structural analysis elucidates how a single residue's altered chirality gives rise to markedly distinct tubular structures and sheds light on the mechanisms underlying the pH-dependent gelation of LL- and LD-tubes. The understanding of dipeptide packing and gelation mechanisms provides insights for the rational design of 2NapFF derivatives, enabling the modulation of micellar dimensions. |
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手法 | EM (らせん対称) |
解像度 | 3.3 Å |
構造データ | ![]() EMDB-42434: Cryo-EM of (L, L)-2NapFF micelle ![]() EMDB-42436: Cryo-EM of (L,D)-2NapFF micelle |
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