Unknown

Dataset Information

0

"Click" immobilization of a VEGF-mimetic peptide on decellularized endothelial extracellular matrix to enhance angiogenesis.


ABSTRACT: We show that coating of decellularized extracellular matrix (DC-ECM) on substrate surfaces is an efficient way to generate a platform mimicking the native ECM environment. Moreover, the DC-ECM can be modified with a peptide (QK) mimicking vascular endothelial growth factor without apparently compromising its integrity. The modification was achieved through metabolic incorporation of a "clickable" handle to DC-ECM followed by rapid attachment of the QK peptide with an azido tag using copper-catalyzed click reaction. The attachment of the QK peptide on to DC-ECM in this way further enhanced the angiogenic responses (formation of branched tubular networks) of endothelial cells.

SUBMITTER: Wang L 

PROVIDER: S-EPMC4059262 | biostudies-other | 2014 Jun

REPOSITORIES: biostudies-other

altmetric image

Publications

"Click" immobilization of a VEGF-mimetic peptide on decellularized endothelial extracellular matrix to enhance angiogenesis.

Wang Lin L   Zhao Meirong M   Li Siheng S   Erasquin Uriel J UJ   Wang Hao H   Ren Li L   Chen Changyi C   Wang Yingjun Y   Cai Chengzhi C  

ACS applied materials & interfaces 20140501 11


We show that coating of decellularized extracellular matrix (DC-ECM) on substrate surfaces is an efficient way to generate a platform mimicking the native ECM environment. Moreover, the DC-ECM can be modified with a peptide (QK) mimicking vascular endothelial growth factor without apparently compromising its integrity. The modification was achieved through metabolic incorporation of a "clickable" handle to DC-ECM followed by rapid attachment of the QK peptide with an azido tag using copper-catal  ...[more]

Similar Datasets

| S-EPMC4547390 | biostudies-literature
| S-EPMC3789176 | biostudies-literature
| S-EPMC4801146 | biostudies-literature
| S-EPMC3408574 | biostudies-literature
| S-EPMC5352540 | biostudies-literature
| S-EPMC3937369 | biostudies-literature
| S-EPMC8102489 | biostudies-literature
| S-EPMC7654553 | biostudies-literature