Hemoglobin protein hollow shells fabricated through covalent layer-by-layer technique
- Beijing National Laboratory for Molecular Sciences (BNLMS), International Joint Lab, CAS Key Lab of Colloid and Interface Science, Institute of Chemistry, Chinese Academy of Sciences, Zhong Guan Cun, Bei Yi Jie No 2, Beijing 100080 (China)
Hemoglobin (Hb) protein microcapsules held together by cross-linker, glutaraldehyde (GA), were successfully fabricated by covalent layer-by-layer (LbL) technique. The Schiff base reaction occurred on the colloid templates between the aldehyde groups of GA and free amino sites of Hb results in the formation of GA/Hb microcapsules after the removal of the templates. The structure of obtained monodisperse protein microcapsule was characterized by transmission electron microscopy (TEM) and confocal laser scanning microscopy (CLSM). The UV-Vis spectra measurements demonstrate the existence of Hb in the assembled capsules. Cyclic voltammetry (CV) and potential-controlled amperometric measurements (I-t curve) confirm that hemoglobin microcapsules after fabrication remain their heme electroactivity. Moreover, direct electron transfer process from protein to electrode surface was performed to detect the heme electrochemistry without using any mediator or promoter. The experiments of fluorescence recovery after photobleaching (FRAP) by CLSM demonstrate that the hemoglobin protein microcapsules have an improved permeability comparing to the conventional polyelectrolyte microcapsules.
- OSTI ID:
- 20979823
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 354, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2006.12.223; PII: S0006-291X(06)02833-6; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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