Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C

Konar AD, Vass E, Hollosi M, Majer Z, Grueber G, Frese K, Sewald N (2013)
Chemistry & Biodiversity 10(5): 942-951.

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The efrapeptins, a family of naturally occurring peptides with inhibitory activities against ATPases, contain several ,-disubstituted -amino acids such as -aminoisobutyric acid (Aib) or isovaline (Iva) besides pipecolic acid (Pip), -Ala, Leu, Gly, and a C-terminal heterocyclic residue. Secondary -amino acids such as proline are known to stabilize discrete conformations in peptides. A similar influence is ascribed to N-alkyl -amino acids. We synthesized two efrapeptin C analogs with replacement of Pip by N-methyl-L-alanine (MeAla) using a combination of solid- and solution-phase techniques in a fragment-condensation strategy to compare the conformational bias of both secondary amino acids. The solution conformation was investigated by vibrational circular dichroism (VCD) to probe whether the analogs adopt a 310-helical conformation. The MeAla-containing analogs [MeAla1,3]efrapeptin C and [MeAla1,3,11]efrapeptin C inhibit ATP hydrolysis by the A3B3 complex of A1A0-ATP synthase from Methanosarcina mazei Go1.
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Konar AD, Vass E, Hollosi M, et al. Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C. Chemistry & Biodiversity. 2013;10(5):942-951.
Konar, A. D., Vass, E., Hollosi, M., Majer, Z., Grueber, G., Frese, K., & Sewald, N. (2013). Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C. Chemistry & Biodiversity, 10(5), 942-951. doi:10.1002/cbdv.201300086
Konar, A. D., Vass, E., Hollosi, M., Majer, Z., Grueber, G., Frese, K., and Sewald, N. (2013). Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C. Chemistry & Biodiversity 10, 942-951.
Konar, A.D., et al., 2013. Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C. Chemistry & Biodiversity, 10(5), p 942-951.
A.D. Konar, et al., “Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C”, Chemistry & Biodiversity, vol. 10, 2013, pp. 942-951.
Konar, A.D., Vass, E., Hollosi, M., Majer, Z., Grueber, G., Frese, K., Sewald, N.: Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C. Chemistry & Biodiversity. 10, 942-951 (2013).
Konar, Anita Dutt, Vass, Elemer, Hollosi, Miklos, Majer, Zsuzsanna, Grueber, Gerhard, Frese, Katrin, and Sewald, Norbert. “Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl-L-alanine in Efrapeptin C”. Chemistry & Biodiversity 10.5 (2013): 942-951.
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