199783-36-3

Upstream product

• 221285-92-3 tert-butyl (S)-3-methyl-2-(2-nitrophenylsulfonamido)butanoate 
• 1694-92-4 2-Nitrobenzenesulfonyl chloride 
• 13518-40-6 L-valine tert-butylester hydrochloride 

Downstream Products

• 270072-08-7 (S)-2-[Benzyl-(2-nitro-benzenesulfonyl)-amino]-3-methyl-butyric acid 
• 1613043-99-4 methyl (S)-3-(1H-indol-3-yl)-2-{(S)-3-isopropyl-4-[(2-nitrophenyl)sulfonyl]-2-oxopiperazin-1-yl}propanoate 
• 1613044-00-0 (S)-3-(1H-indol-3-yl)-2-{(S)-3-isopropyl-4-[(2-nitrophenyl)sulfonyl]-2-oxopiperazin-1-yl} propanoic acid 
• 1613043-80-3 tert-butyl {(S)-1-{[(S)-1-({(S)-1-[(S)-4-{(S)-1-[(2-amino-2-oxoethyl)amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl}-2-isopropyl-3-oxopiperazin-1-yl]-3-(tert-butoxy)-1-oxopropan-2-yl}amino)-1-oxo-3-phenylpropan-2-yl]amino}-3-[4-(tert-butoxy)phenyl]-1-oxopropan-2-yl}carbamate 
• 1613043-81-4 (S)-2-amino-N-[(S)-1-({(S)-1-[(S)-4-{(S)-1-[(2-amino-2-oxoethyl)amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl}-2-isopropyl-3-oxopiperazin-1-yl]-3-hydroxy-1-oxopropan-2-yl}amino)-1-oxo-3-phenylpropan-2-yl]-3-(4-hydroxyphenyl)propanamide 
• 1613043-75-6 methyl (S)-3-(1H-indol-3-yl)-2-[(S)-3-methyl-2-(2-nitrophenylsulfonamido)butanamido]propanoate 
• 1350538-44-1 (4R,9R,12S)-12-isopropyl-3,13-bis(2-nitrobenzenesulfonyl)-19-oxy-3,10,13,19-tetraazatricyclo[13.3.1.0(4,9)] nonadeca-1⁽¹⁹⁾,15,17-trien-11-one 
• 1350538-38-3 (4R,9R,12S)-12-isopropyl-3,13-bis(2-nitrobenzenesulfonyl)-3,10,13,19-tetraazatricyclo[13.3.1.0(4,9)]nonadeca-1⁽¹⁹⁾,15,17-trien-11-one 
• 1350538-53-2 C₃₅H₄₃N₇O₁₁S₂ 
• 1350538-48-5 (2S,2S')-N,N'-((1R,2R)-cyclohexan-1,2-diyl)bis(3-methyl-2-(2-nitrophenylsulfonamido)butanamide) 
• 1350538-35-0 (S)-3-methyl-2-(2-nitrophenylsulfonamido)-N-((1R,2R)-2-(2-nitrophenylsulfonamido)cyclohexyl)-butanamide 
• 1065276-60-9 C₂₅H₂₇N₃O₇S 
• 96349-67-6 methyl 2,2-dichloro-3-hydroxy-3-(4-methoxyphenyl)propanoate 

Relevant academic research and scientific papers

Structural prerequisites for receptor binding of helicokinin I, a diuretic insect neuropeptide from helicoverpa zea

In insects essential physiological processes such as muscle activity or water balance are controlled by neuropeptides. However, owing to their metabolic instability and adverse physicochemical properties peptides are unsuited as crop protection agents. Helicokinin I, a diuretic neuropeptide of cotton pest Helicoverpa zea represents a most promising target for the design of neuropeptide mimetics. Several helicokinin analogues containing scaffolds with varying rigidity and different orientations of the N- and C-terminal peptide chains were synthesized and tested for receptor binding. Additional conformational analyses by NMR spectroscopy in a membrane-mimicking environment together with MD simulations provide a deeper insight into the structural requirements for receptor binding and explain the remarkable activity of a macrocyclic helicokinin I derivative. A delicate balance of rigidity and flexibility makes the difference between activity and inactivity. Detailed conformational studies of analogues of the diuretic insect-neuropeptide helicokinin I containing diverse cyclic scaffolds with different flexibility and orientation of the N- and C-termini provide a better understanding of the structural requirements for receptor binding. Copyright