PMID- 21683437
OWN - NLM
STAT- MEDLINE
DCOM- 20111109
LR  - 20211020
IS  - 1878-5905 (Electronic)
IS  - 0142-9612 (Print)
IS  - 0142-9612 (Linking)
VI  - 32
IP  - 27
DP  - 2011 Sep
TI  - Controlled biodegradation of self-assembling beta-hairpin peptide hydrogels by 
      proteolysis with matrix metalloproteinase-13.
PG  - 6471-7
LID - 10.1016/j.biomaterials.2011.05.052 [doi]
AB  - Controlled biodegradation specific to matrix metalloproteinase-13 was 
      incorporated into the design of self-assembling beta-hairpin peptide hydrogels. 
      Degrading Peptides (DP peptides) are a series of five peptides that have varying 
      proteolytic susceptibilities toward MMP-13. These peptides undergo 
      environmentally triggered folding and self-assembly under physiologically 
      relevant conditions (150 mm NaCl, pH 7.6) to form self-supporting hydrogels. In 
      the presence of enzyme, gels prepared from distinct peptides are degraded at 
      rates that differ according to the primary sequence of the single peptide 
      comprising the gel. Material degradation was monitored by oscillatory shear 
      rheology over the course of 14 days, where overall degradation of the gels vary 
      from 5% to 70%. Degradation products were analyzed by HPLC and identified by 
      electrospray-ionization mass spectrometry. This data shows that proteolysis of 
      the parent peptides constituting each gel occurs at the intended sequence 
      location. DP hydrogels show specificity to MMP-13 and are only minimally cleaved 
      by matrix metalloproteinase-3 (MMP-3), another common enzyme present during 
      tissue injury. In vitro migration assays performed with SW1353 cells show that 
      migration rates through each gel differs according to peptide sequence, which is 
      consistent with the proteolysis studies using exogenous MMP-13.
CI  - Published by Elsevier Ltd.
FAU - Giano, Michael C
AU  - Giano MC
AD  - National Cancer Institute, Center for Cancer Research, Frederick, MD 21701, USA.
FAU - Pochan, Darrin J
AU  - Pochan DJ
FAU - Schneider, Joel P
AU  - Schneider JP
LA  - eng
GR  - ZIA BC011313-01/ImNIH/Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
DEP - 20110616
PL  - Netherlands
TA  - Biomaterials
JT  - Biomaterials
JID - 8100316
RN  - 0 (Hydrogels)
RN  - 0 (Peptides)
RN  - EC 3.4.24.- (Matrix Metalloproteinase 13)
SB  - IM
MH  - Amino Acid Sequence
MH  - Biodegradation, Environmental
MH  - Cell Line, Tumor
MH  - Humans
MH  - Hydrogels/*chemistry
MH  - Matrix Metalloproteinase 13/*metabolism
MH  - Molecular Sequence Data
MH  - Peptides/*chemistry/*metabolism
MH  - *Protein Processing, Post-Translational
MH  - Protein Structure, Secondary
MH  - Rheology
PMC - PMC3155979
MID - NIHMS306387
EDAT- 2011/06/21 06:00
MHDA- 2011/11/10 06:00
PMCR- 2012/09/01
CRDT- 2011/06/21 06:00
PHST- 2011/04/25 00:00 [received]
PHST- 2011/05/15 00:00 [accepted]
PHST- 2011/06/21 06:00 [entrez]
PHST- 2011/06/21 06:00 [pubmed]
PHST- 2011/11/10 06:00 [medline]
PHST- 2012/09/01 00:00 [pmc-release]
AID - S0142-9612(11)00584-9 [pii]
AID - 10.1016/j.biomaterials.2011.05.052 [doi]
PST - ppublish
SO  - Biomaterials. 2011 Sep;32(27):6471-7. doi: 10.1016/j.biomaterials.2011.05.052. 
      Epub 2011 Jun 16.