Porous Peptide Complexes by a Folding‐and‐Assembly Strategy

Sawada, Tomohisa; Yamagami, Motoya; Akinaga, Shuji; Miyaji, Tatsuki; Fujita, Makoto

doi:10.1002/asia.201700458

Cited by 30 publications

(14 citation statements)

References 26 publications

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“…SEM imaging of this last sample showed threads ( Figure 3) and, a much more surprising result, the formation of a porous cylindrical structure (Figure 3), a few microns in diameter. Porous and cavity structures are vital in the assembly and proper functioning of proteins [35]. Additionally, such porous and multi-chambered structures are feasible candidates for primitive abiotic cellularity due to their energy capture and conversion capacity [36].…”

Section: Complex Structure Formation and Consequences For The Studiesmentioning

confidence: 99%

Shock Processing of Amino Acids Leading to Complex Structures—Implications to the Origin of Life

et al. 2020

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The building blocks of life, amino acids, are believed to have been synthesized in the extreme conditions that prevail in space, starting from simple molecules containing hydrogen, carbon, oxygen and nitrogen. However, the fate and role of amino acids when they are subjected to similar processes largely remain unexplored. Here we report, for the first time, that shock processed amino acids tend to form complex agglomerate structures. Such structures are formed on timescales of about 2 ms due to impact induced shock heating and subsequent cooling. This discovery suggests that the building blocks of life could have self-assembled not just on Earth but on other planetary bodies as a result of impact events. Our study also provides further experimental evidence for the ‘threads’ observed in meteorites being due to assemblages of (bio)molecules arising from impact-induced shocks.

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Section: Complex Structure Formation and Consequences For The Studiesmentioning

confidence: 99%

Shock Processing of Amino Acids Leading to Complex Structures—Implications to the Origin of Life

et al. 2020

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“…Tripeptide ligands 3 , 5 , 7 , and 9 were synthesised using a route analogous to that published previously 25 . Detailed procedures and characterisation data of all compounds are shown in Supplementary Methods and Supplementary Figs.…”

Section: Methodsmentioning

confidence: 99%

Metal–peptide rings form highly entangled topologically inequivalent frameworks with the same ring- and crossing-numbers

et al. 2019

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With increasing ring-crossing number (c), knot theory predicts an exponential increase in the number of topologically different links of these interlocking structures, even for structures with the same ring number (n) and c. Here, we report the selective construction of two topologies of 12-crossing peptide [4]catenanes (n = 4, c = 12) from metal ions and pyridine-appended tripeptide ligands. Two of the 100 possible topologies for this structure are selectively created from related ligands in which only the tripeptide sequence is changed: one catenane has a T2-tetrahedral link and the other a three-crossed tetrahedral link. Crystallographic studies illustrate that a conformational difference in only one of the three peptide residues in the ligand causes the change in the structure of the final tetrahedral link. Our results thus reveal that peptide-based folding and assembly can be used for the facile bottom-up construction of 3D molecular objects containing polyhedral links.

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“…Such peptides are employed to promote folding during the metal‐coordination‐driven assembly process to build well‐defined supramolecular architectures. In particular, the importance of the balance between conformational robustness and flexibility of the peptide ligand has been described well in the work of Fujita et al [6b] …”

Section: Introductionmentioning

confidence: 92%

Conformational Adaptation of β‐Peptide Foldamers for the Formation of Metal–Peptide Frameworks

et al. 2021

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Metal‐coordinated frameworks derived from small peptidic ligands have received much attention thanks to peptides’ vast structural and functional diversity. Various peptides with partial conformational preferences have been used to build metal–peptide frameworks, however, the use of conformationally constrained β‐peptide foldamers has not been explored yet. Herein we report the first metal‐coordination‐mediated assembly of β‐peptide foldamers with 12‐helical folding propensity. The coordination of Ag+ to the terminal pyridyl moieties afforded a set of metal–peptide frameworks with unique entangled topologies. Interestingly, formation of the network structures was accompanied by notable conformational distortions of the foldamer ligands. As the first demonstration of new metal–peptide frameworks built from modular β‐peptide foldamers, we anticipate that this work will be an important benchmark for further structural evolution and mechanistic investigation.

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Porous Peptide Complexes by a Folding‐and‐Assembly Strategy

Cited by 30 publications

References 26 publications

Shock Processing of Amino Acids Leading to Complex Structures—Implications to the Origin of Life

Shock Processing of Amino Acids Leading to Complex Structures—Implications to the Origin of Life

Metal–peptide rings form highly entangled topologically inequivalent frameworks with the same ring- and crossing-numbers

Conformational Adaptation of β‐Peptide Foldamers for the Formation of Metal–Peptide Frameworks

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