We report the
synthe
si
s and char
acterization of multifunctional peptide
s compri
sed of a hydrogel forming β-
sheet peptide
segment and a matrix metalloproteina
se 2
sub
strate containing a propargylglycinyl linker that i
s further derivatized with an RGD peptide
sequence
via “click” chemi
stry. In contra
st to currently known
sy
stem
s, the
se multifunctional peptide
s formed gel
s that are
stiffer than tho
se formed by their re
spective precur
sor
s. All the peptide
s showed rever
sible thermore
spon
sive propertie
s, which render them a
s suitable lead
sy
stem
s for a variety of po
ssible biomedical application
s.
sSec_2">Statement of Significance
sp0015">In general, it has been frequently observed that chemical biofunctionalization of peptide hydrogels adversely affects peptide assembly, hydrogel formation or mechanical properties, which severely compromises their application. A functionalization protocol that allows to generate peptide hydrogels that display significantly improved mechanical properties over their unfunctionalized counterparts is reported in this work. These peptides also showed thermoresponsive viscoelastic characteristics, including an example of a peptide hydrogel that displays lower critical solution temperature behaviour.