02611naa a2200337 a 450000100080000000500110000800800410001902400520006010000280011224501610014026000090030152015890031065000130189965000220191265000140193465300160194865300160196465300210198065300180200165300250201965300250204465300220206965300220209170000180211370000230213170000210215470000210217570000140219670000190221077300440222921614342024-01-29       2023    bl uuuu     u00u1 u    #d7 ahttps://doi.org/10.1007/s00726-023-03309-x2DOI1 aGUIMARÃES, C. F. R. C.  aOptimizing the synthesis of dimeric peptidesbinfluence of the reaction medium and effects that modulate kinetics and reaction yield.h[electronic resource]  c2023  aPeptides are remarkably interesting alternatives to several applications. In particular, antimicrobial sequences have raised major interest of the scientifc community due to the resistance acquired by commonly used antibiotics. Amongst these, some dimeric peptides have shown very promising characteristics as strong biological activities and resistance against degradation by peptidases. However, despite such promising characteristics, a relatively small number of studies address dimeric peptides, mainly due to the synthesis-related obstacles in their production, whereas the well-implemented routines of solid phase peptide synthesis—which includes the possibility of automation—makes life signifcantly easier. Here, we present kinetic investigations of the dimerization of a cysteine-containing sequence to obtain the homodimeric antimicrobial peptide homotarsinin. Based on the structural and membrane interaction data already available for the dimer and its monomeric chain, we have proposed distinct dimerization protocols in selected environments, namely, aqueous bufer, TFE:H2O and micellar solutions. The experimental results were adjusted by a theoretical model. Both the kinetic profles and the reaction yields are dependent on the reaction medium, clearly indicating that aggregation, peptide structure, and peptide–membrane interactions play major roles in the formation of the disulfde bond. Finally, the rationalization of the diferent aspects addressed here is expected to contribute to research and applications that demand the obtainment of dimeric peptides  aKinetics  aEnergia Cinética  aPeptídeo  aAggregation  aAgregação  aDimeric peptides  aDisulfde bond  aEstrutura peptídica  aLigação dissulfeto  aPeptide structure  aPeptide synthesis1 aFÉLIX. A. S.1 aBRANDÃO, T. A. S.1 aBEMQUERER, M. P.1 aPILÓ-VELOSO, D.1 aVERLY, R.1 aRESENDE, J. M.  tAmino Acidsgv. 55, p. 1201-1212, 2023.