Sponge-Like Behaviour in Isoreticular Cu(Gly-His-X) Peptide-Based Porous Materials

نویسندگان

  • Carlos Martí-Gastaldo
  • John E Warren
  • Michael E Briggs
  • Jayne A Armstrong
  • K Mark Thomas
  • Matthew J Rosseinsky
چکیده

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.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Isoreticular expansion of metal-organic frameworks with triangular and square building units and the lowest calculated density for porous crystals.

The concept and occurrence of isoreticular (same topology) series of metal-organic frameworks (MOFs) is reviewed. We describe the preparation, characterization, and crystal structures of three new MOFs that are isoreticular expansions of known materials with the tbo (Cu(3)(4,4',4''-(benzene-1,3,5-triyl-tris(benzene-4,1-diyl))tribenzoate)(2), MOF-399) and pto topologies (Cu(3)(4,4',4''-(benzene-...

متن کامل

Design and spectroscopic characterization of peptide models for the plastocyanin copper-binding loop.

The Cu(II)- and Co(II)-binding properties of two peptides, designed on the basis of the active site sequence and structure of the blue copper protein plastocyanin, are explored. Peptide BCP-A, Ac-Trp-(Gly)(3)-Ser-Tyr-Cys-Ser-Pro-His-Gln-Gly-Ala-Gly-Met-(Gly )(3)-His-(Gly)(2)-Lys-CONH(2), conserves the Cu-binding loop of plastocyanin containing three of the four copper ligands and has a flexible...

متن کامل

Hydroxyapatite-Hardystonite nanocomposite scaffolds prepared by the replacing the polyurethane polymeric sponge technique for tissue engineering applications

Objective (s): Silicate bioceramics containing Zn and Ca like hardystonite (Hr) with chemical formula Ca2ZnSi2O7 has attracted the attention of researchers in biomedical field due to its remarkable biological and mechanical properties. The new generation of bioceramics can applied in bone tissue engineering to substitute with infected bone. However, these zirconium-silicate bioceramics have pro...

متن کامل

Amino acid sequences of three bombesin-like peptides from canine intestine extracts.

Amino acid sequences of three canine bombesin-like peptides were determined after sequential purification of an extract obtained from 820 g of intestinal muscle. These three peptides contained 27, 23, and 10 amino acid residues. The sequences of the two shorter forms were identical to the corresponding carboxyl-terminal sequence of the heptacosapeptide. The sequence of the largest peptide is H2...

متن کامل

Interaction of Cu(II)with His-Val-Gly-Asp and of Zn(II) with His-Val-His, Two Peptides at the Active Site of Cu,Zn-Superoxide Dismutase

His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). We have already studied the interaction of His-Val-His=A (copper binding site) with Cu(II) and of His-Val-Gly-Asp=B (zinc binding site) with Zn(II). As a continuation of this work and for comparison purposes we have also studied the interaction of ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره 21  شماره 

صفحات  -

تاریخ انتشار 2015