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This analysis highlighted the unique binding potential of exendin 2029, suggesting its efficacy as a targeted TRPV1 blocker derived from exendin 939

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The cryo-EM electron potential map revealed the VP0, VP1 and VP3 capsid protein subunits of the PV3-SC8 VLP to be well ordered and there was an unambiguous feature for bound GSH in the interprotomer pocket formed between VP1 subunits from two adjacent protomers and VP3 from a single protomer (Fig