Sponge-Like Behaviour in Isoreticular Cu(Gly-His-X) Peptide-Based Porous Materials.
Martí-Gastaldo. Carlos C; Warren. John E JE; Briggs. Michael E ME; Armstrong. Jayne A JA; Thomas. K Mark KM; Rosseinsky. Matthew J MJ
Key Findings
- Copper‑linked peptide crystals form porous, sponge‑like frameworks that collapse on drying and reopen with water vapor.
- Water vapor, but not CO2, can restore the original open‑channel structure of these materials.
- The lysine side‑chain in the framework can be post‑synthetically turned into a urea‑functional group.
Practical Outcomes
- These findings are interesting for material science and could lead to new types of reusable adsorbents or sensors, but they do not provide any direct health‑related advice, dosage guidance, or performance‑enhancing protocols for biohackers.
Summary
Scientists made two new sponge‑like, 3‑dimensional structures by linking short protein pieces (Gly‑His‑Gly and Gly‑His‑Lys) with copper. These materials can collapse when dried and then reopen when they see water vapor, but they don’t recover when exposed to carbon dioxide. The researchers also showed they can chemically modify the lysine part after the material is built.
Abstract
We report two isoreticular 3D peptide-based porous frameworks formed by coordination of the tripeptides Gly-L-His-Gly and Gly-L-His-L-Lys to Cu(II) which display sponge-like behaviour. These porous materials undergo structural collapse upon evacuation that can be reversed by exposure to water vapour, which permits recovery of the original open channel structure. This is further confirmed by sorption studies that reveal that both solids exhibit selective sorption of H2 O while CO2 adsorption does not result in recovery of the original structures. We also show how the pendant aliphatic amine chains, present in the framework from the introduction of the lysine amino acid in the peptidic backbone, can be post-synthetically modified to produce urea-functionalised networks by following methodologies typically used for metal-organic frameworks built from more rigid "classical" linkers.
Study Information
pubmed
2015
2015-09-25T00:00:00.000Z
10.1002/chem.201502098
35
67