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. Author manuscript; available in PMC: 2012 Dec 13.
Published in final edited form as: J Med Chem. 2011 Oct 3;54(20):7375–7384. doi: 10.1021/jm2009937

Table 1.

Analytical data of synthesized multimers.

Compounda Linker Mass Spectrumb HPLCc, tR (min)
Ion Calc. Obsd.
Ac-MSH(4) - (M+1)+ 686.3482 686.6389 9.75
NB297 No linker (M+5)5+ 650.1385 650.1376 12.37
NB298 (Gly-Pro)1 (M+6)6+ 647.4978 647.4982 12.97
NB299 (Gly-Pro)2 (M+6)6+ 724.5349 724.5359 12.90
NB300 (Gly-Pro)3 (M+6)6+ 801.5720 801.5709 12.86
NB301 β-Ala (M+6)6+ 577.4685 577.4683 12.90
NB302 (β-Ala)2 (M+6)6+ 612.9871 612.9861 12.83
NB341 No linker (M+5)5+ 548.0752 548.0752 12.94
NB342 β-Ala (M+5)5+ 590.6974 590.6969 12.90
NB397 No linker (M+2)2+ 689.3679 689.3666 11.58
NB399 No linker (M+4)4+ 578.8050 578.8053 12.62
a

NB297 to NB302 were synthesized using peptide (A) and NB341 to NB399 were synthesized using peptide (B). NB397 is the monovalent ligand and NB399 is the bivalent ligand.

b

Maldi-TOF or ESI-MS.

c

Peptides were eluted with a linear gradient from 0 to 100% acetonitrile containing 0.1%TFA in 30 min at 1mL/min. The purity of all peptides determinec by HPLC was ≥ 95%.