I'm trying to develop a hydrogel which can release proteins at a controlled rate.
I'm currently using 4 arm PEG maleimide (10 & 20 kDa) and 2 kDa PEG dithiol has the crosslinker via micheal type addition reaction.
According to Zustiak and Leach (2010) Biomacromolecules, 11, 1348-1357 - the Mw of a crosslinker is related to the degredation of the hydrogel. they have results showing hydrogels crosslinked with 8 kDa crosslinker degraded faster then 2 kDa crosslinker.
So am i right to assume if i use 1kDa PEG dithiol the PEG Malemidie will be more stable?
Has anyone used other crosslinkers apart from PEG Dithiol?
Thanks.
Generally, your chemistry is not optimal. Please consider that, if there are some free maleimide groups present in the hydrogel, they may react with SH functions or NH2 groups of the included protein. Additionally, what about the smell??
I recommend to use suitable Jeffamine ® (PEG diamine) instead of mercaptans. They also react via Michael Addition. What about acryl-chemistry?
Good luck.
If the gel is strongly crosslinked, the crosslinked density is just the inverse of the number of monomers between two consecutive crosslinks. Now, for weakly crosslinked gels, this density is essentially the inverse of the molecular weight of crosslinked chains.
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