Abstract
To determine local chirality driven conformational preferences of small aminocyclobutane-1-carboxylic acid derivatives, X-(ACBA) n -Y, their matrix-isolation IR spectra were recorded and analyzed. For the very first time model systems of this kind were deposited in a frozen (~10 K) noble gas matrix to reduce line width and thus, the recorded sharp vibrational lines were analyzed in details. For cis-(S,R)-1 monomer two “zigzag” conformers composed of either a six or an eight-membered H-bonded pseudo ring was identified. For trans-(S,S)-2 stereoisomer a zigzag of an eight-membered pseudo ring and a helical building unit were determined. Both findings are fully consistent with our computational results, even though the relative conformational ratios were found to vary with respect to measurements. For the dimers (S,R,S,S)-3 and (S,S,S,R)-4 as many as four different cis,trans and three different trans,cis conformers were localized in their matrix-isolation IR (MI-IR) spectra. These foldamers not only agree with the previous computational and NMR results, but also unambiguously show for the first time the presence of a structure made of a cis,trans conformer which links a “zigzag” and a helical foldamer via a bifurcated H-bond. The present work underlines the importance of MI-IR spectroscopy, applied for the first time for triamides to analyze the conformational pool of small biomolecules. We have shown that the local chirality of a β-amino acid can fully control its backbone folding preferences. Unlike proteogenic α-peptides, β- and especially (ACBA) n type oligopeptides could thus be used to rationally design and influence foldamer’s structural preferences.
Similar content being viewed by others
References
Baker J, Jarzecki AA, Pulay P (1998) Direct scaling of primitive valence force constants: an alternative approach to scaled quantum mechanical force fields. J Phys Chem A 102(8):1412–1424
Baker J, Wolinski K, Malagoli M, Kinghorn D, Wolinski P, Magyarfalvi G, Saebo S, Janowski T, Pulay P (2009) Quantum chemistry in parallel with PQS. J Comput Chem 30(2):317–335
Bazsó G, Magyarfalvi G, Tarczay G (2012a) Near-infrared laser induced conformational change and UV laser photolysis of glycine in low-temperature matrices: observation of a short-lived conformer. J Mol Struct 1025:33–42
Bazsó G, Magyarfalvi G, Tarczay G (2012b) Tunneling lifetime of the ttc/VIp conformer of glycine in low-temperature matrices. J Phys Chem A 116(43):10539–10547
Bazsó G, Najbauer EE, Magyarfalvi G, Tarczay G (2013) Near-infrared laser induced conformational change of alanine in low-temperature matrixes and the tunneling lifetime of its conformer VI. J Phys Chem A 117(9):1952–1962
Becke AD (1993) Density-functional thermochemistry. III. The role of exact exchange. J Chem Phys 98(7):5648–5652
Beke T, Somlai C, Perczel A (2006) Toward a rational design of β-peptide structures. J Comput Chem 27(1):20–38
Beke T, Somlai C, Magyarfalvi G, Perczel A, Tarczay G (2009) Chiral and achiral fundamental conformational building units of β-peptides: a matrix isolation conformational study on Ac-β-HGly-NHMe and Ac-β-HAla-NHMe. J Phys Chem B 113(22):7918–7926
Binkley JS, Pople JA, Hehre WJ (1980) Self-consistent molecular orbital methods. 21. Small split-valence basis sets for first-row elements. J Am Chem Soc 102(3):939–947
Boeckx B, Maes G (2012a) Potential energy surface and matrix isolation FT-IR study of isoleucine. J Phys Chem A 116(12):3247–3258
Boeckx B, Maes G (2012b) The conformational behavior and H-bond structure of asparagine: a theoretical and experimental matrix-isolation FT-IR study. Biophys Chem 165–166:62–73
Boeckx B, Maes G (2012c) Experimental and theoretical observation of different intramolecular H-bonds in lysine conformations. J Phys Chem B 116(41):12441–12449
Boeckx B, Maes G (2012d) Comparison of the conformational behavior of amino acids and N-acetylated amino acids: a theoretical and matrix-isolation FT-IR study of N-acetylglycine. J Phys Chem A 116(8):1956–1965
Boeckx B, Maes G (2012e) Estimation of the rotamerization constants of different conformations of N-acetylalanine: a theoretical and matrix-isolation FT-IR study. Spectrochim Acta A 86:366–374
Boeckx B, Ramaekers R, Maes G (2010) A theoretical and matrix-isolation FT-IR investigation of the conformational landscape of N-acetylcysteine. J Mol Spectrosc 261(2):73–81
Boeckx B, Ramaekers R, Maes G (2011) The influence of the peptide bond on the conformation of amino acids: a theoretical and FT-IR matrix-isolation study of N-acetylproline. Biophys Chem 159(2–3):247–256
Dobrowolski JC, Jamróz MH, Kołos R, Rode JE, Sadlej J (2007) Theoretical prediction and the First IR matrix observation of several l-cysteine molecule conformers. Chem Phys Chem 8(7):1085–1094
Dobrowolski JC, Jamróz HM, Kolos R, Rode JE, Sadlej J (2008) IR low-temperature matrix and ab initio study on β-alanine conformers. Chem Phys Chem 9(14):2042–2051
Fábri C, Szidarovszky T, Magyarfalvi G, Tarczay G (2011) Gas-phase and Ar-matrix SQM scaling factors for various DFT functionals with basis sets including polarization and diffuse functions. J Phys Chem A 115(18):4640–4649
Fernandes C, Faure S, Pereira E, Théry V, Declerck V, Guillot R, Aitken DJ (2010) 12-helix folding of cyclobutane β-amino acid oligomers. Org Lett 12(16):3606–3609
Frisch MJ, Trucks GW, Schlegel HB, Scuseria GE, Robb MA, Cheeseman JR, Scalmani G, Barone V, Mennucci B, Petersson GA, Nakatsuji H, Caricato M, Li X, Hratchian HP, Izmaylov AF, Bloino J, Zheng G, Sonnenberg JL, Hada M, Ehara M, Toyota K, Fukuda R, Hasegawa J, Ishida M, Nakajima T, Honda Y, Kitao O, Nakai H, Vreven T, Montgomery Jr. JA, Peralta JE, Ogliaro F, Bearpark M, Heyd JJ, Brothers E, Kudin KN, Staroverov VN, Kobayashi R, Normand J, Raghavachari K, Rendell A, Burant JC, Iyengar SS, Tomasi J, Cossi M, Rega N, Millam JM, Klene M, Knox JE, Cross JB, Bakken V, Adamo C, Jaramillo J, Gomperts R, Stratmann RE, Yazyev O, Austin AJ, Cammi R, Pomelli C, Ochterski JW, Martin RL, Morokuma K, Zakrzewski VG, Voth GA, Salvador P, Dannenberg JJ, Dapprich S, Daniels AD, Farkas Ö, Foresman JB, Ortiz JV, Cioslowski J, Fox DJ (2009) Gaussian 09, Revision A.1. Gaussian Inc, Wallingford, CT
Góbi S, Knapp K, Vass E, Majer Z, Magyarfalvi G, Hollósi M, Tarczay G (2010) Is β-homo-proline a pseudo-γ-turn forming element of β-peptides? An IR and VCD spectroscopic study on Ac-β-HPro-NHMe in cryogenic matrices and solutions. Phys Chem Chem Phys 12(41):13603–13615
Gorrea E, Pohl G, Nolis P, Celis S, Burusco KK, Branchadell V, Perczel A, Ortuño RM (2012) Secondary structure of short β-peptides as the chiral expression of monomeric building units: a rational and predictive model. J Org Chem 77(21):9795–9806
Grenie Y, Garrigou-Lagrange C (1972) Infrared spectra of glycine isotopic species isolated in an argon or nitrogen matrix. J Mol Spectrosc 41(2):240–246
Grenie Y, Lassegues JC, Garrigou-Lagrange C (1970) Infrared spectrum of matrix-isolated glycine. J Chem Phys 53(7):2980–2982
Grenie Y, Avignon M, Garrigou-Lagrange C (1975) Molecular structure study of dipeptides isolated in an argon matrix by infrared spectroscopy. J Mol Struct 24(2):293–307
Halgren TA (1996) Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J Comput Chem 17(5–6):490–519
Hehre WJ, Ditchfield R, Pople JA (1972) Self-consistent molecular orbital methods. XII. Further extensions of gaussian-type basis sets for use in molecular orbital studies of organic molecules. J Chem Phys 56(5):2257–2261
Ivanov AYu, Plokhotnichenko AM, Izvekov V, Sheina GG, Blagoi YuP (1997) FTIR investigation of the effect of matrices (Kr, Ar, Ne) on the UV-induced isomerization of the monomeric links of biopolymers. J Mol Struct 408–409:459–462
Ivanov AYu, Sheina G, Blagoi YuP (1999) FTIR spectroscopic study of the UV-induced rotamerization of glycine in the low temperature matrices (Kr, Ar, Ne). Spectrochim Acta Part A 55(1):219–228
Jarmelo S, Lapinski L, Nowak MJ, Carey PR, Fausto R (2005) Preferred conformers and photochemical (λ > 200 nm) reactivity of serine and 3,3-dideutero-serine in the neutral form. J Phys Chem A 109(25):5689–5707
Jarmelo S, Reva ID, Rozenberg M, Carey PR, Fausto R (2006) Low-temperature infrared spectra and hydrogen bonding in polycrystalline dl-serine and deuterated derivatives. Vib Spectr 41(1):73–82
Kaczor A, Reva ID, Proniewicz LM, Fausto R (2006) Importance of entropy in the conformational equilibrium of phenylalanine: a matrix-isolation infrared spectroscopy and density functional theory study. J Phys Chem A 110(7):2360–2370
Kaczor A, Reva ID, Proniewicz LM, Fausto R (2007) Matrix-isolated monomeric tryptophan: electrostatic interactions as nontrivial factors stabilizing conformers. J Phys Chem A 111(15):2957–2965
Lambie B, Ramaekers R, Maes G (2003) On the contribution of intramolecular H-bonding entropy to the conformational stability of alanine conformations. Spectrochim Acta A 59(6):1387–1397
Lambie B, Ramaekers R, Maes G (2004) Conformational behavior of serine: an experimental matrix-isolation FT-IR and theoretical DFT(B3LYP)/6-31++G** study. J Phys Chem A 108(47):10426–10433
Lapinski L, Nowak MJ, Reva ID, Rostkowska H, Fausto R (2010) NIR-laser-induced selective rotamerization of hydroxy conformers of cytosine. Phys Chem Chem Phys 12(33):9615–9618
Lapinski L, Reva I, Nowak MJ, Fausto R (2011) Five isomers of monomeric cytosine and their interconversions induced by tunable UV laser light. Phys Chem Chem Phys 13(20):9676–9684
Lee C, Yang W, Parr RG (1998) Development of the colle-salvetti correlation-energy formula into a functional of the electron density. Phys Rev B 37(2):785–789
Mohamadi F, Richards NG, Guida WC, Liskamp R, Lipton M, Caufield C, Chang G, Hendrickson T, Still WC, MacroModel 7.0 (1990) Macromodel—an integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J Comput Chem 11(4):440–467
Nunes CM, Lapinski L, Fausto R, Reva I (2013) Near-IR laser generation of a high-energy conformer of l-alanine and the mechanism of its decay in a low-temperature nitrogen matrix. J Chem Phys 138(12):125101
Pohl G, Perczel A, Vass E, Magyarfalvi G, Tarczay G (2007) A matrix isolation study on Ac-Gly-NHMe and Ac-l-Ala-NHMe, the simplest chiral and achiral building blocks of peptides and proteins. Phys Chem Chem Phys 9(33):4698–4708
Pohl G, Perczel A, Vass E, Magyarfalvi G, Tarczay G (2008) A matrix isolation study on Ac–l-Pro–NH2: a frequent structural element of β- and γ-turns of peptides and proteins. Tetrahedron 64(9):2126–2133
Pulay P, Fogarasi G, Pongor G, Boggs JE, Vargha A (1983) Combination of theoretical ab initio and experimental information to obtain reliable harmonic force constants. Scaled quantum mechanical (QM) force fields for glyoxal, acrolein, butadiene, formaldehyde, and ethylene. J Am Chem Soc 105(24):7037–7047
Ramaekers R, Pajak J, Rospenk M, Maes G (2005) Matrix-isolation FT-IR spectroscopic study and theoretical DFT(B3LYP)/6-31++G** calculations of the vibrational and conformational properties of tyrosine. Spectrochim Acta Part A 61(7):1347–1356
Reva ID, Plokhotnichenko AM, Stepanian SG, Ivanov AYu, Radchenko ED, Sheina GG, Blagoi YP (1995) The rotamerization of conformers of glycine isolated in inert gas matrices. An infrared spectroscopic study. Chem Phys Lett 232(1–2):141–148 (1995) Erratum. Chem Phys Lett 235(5–6):617–617
Reva ID, Stepanian SG, Plokhotnichenko A, Radchenko ED, Sheina G, Blagoi YuP (1994) Infrared matrix isolation studies of amino acids. Molecular structure of proline. J Mol Struct 318:1–13
Rosado MTS, Duarte MLRS, Fausto R (1997) Vibrational spectra (FT-IR, Raman and MI-IR) of α- and β-alanine. J Mol Struct 410–411:343–348
Sheina GG, Radchenko ED, Ivanov AY, Stepanian SG, Blagoi YP (1988) Oscillating spectra of leucine. Zh Fiz Khim 62:985–990
Stepanian SG, Reva ID, Radchenko ED, Rosado MTS, Duarte MLTS, Fausto R, Adamowicz L (1998a) Matrix-isolation infrared and theoretical studies of the glycine conformers. J Phys Chem A 102(6):1041–1054
Stepanian SG, Reva ID, Radchenko ED, Adamowicz L (1998b) Conformational behavior of α-alanine. Matrix-isolation infrared and theoretical DFT and ab initio study. J Phys Chem A 102(24):4623–4629
Stepanian SG, Reva ID, Radchenko ED, Adamowicz L (1999) Combined matrix-isolation infrared and theoretical DFT and ab initio study of the nonionized valine conformers. J Phys Chem A 103(22):4404–4412
Stepanian SG, Reva ID, Radchenko ED, Adamowicz L (2001) Conformers of nonionized proline. Matrix-isolation infrared and post-hartree-fock ab initio study. J Phys Chem A 105(47):10664–10672
Tarczay G, Góbi S, Vass E, Magyarfalvi G (2009) Model peptide–water complexes in Ar matrix: complexation induced conformation change and chirality transfer. Vib Spectrosc 50(1):21–28
Torres E, Gorrea E, Da Silva E, Nolis P, Branchadell V, Ortuño RM (2009) Prevalence of eight-membered hydrogen-bonded rings in some bis(cyclobutane) β-dipeptides including residues with trans stereochemistry. Org Lett 11(11):2301–2304
Torres E, Gorrea E, Burusco KK, Da Silva E, Nolis P, Rúa F, Boussert S, Díez-Pérez I, Dannenberg S, Izquierdo S, Giralt E, Jaime C, Branchadell V, Ortuño RM (2010) Folding and self-assembling with beta-oligomers based on (1R,2S)-2-aminocyclobutane-1-carboxylic acid. Org Biomol Chem 8(3):564–575
Wierzejewska M, Olbert-Majkut A (2009) Conformational behavior of the simplest dipeptide: formylglycine. Quantum chemical and matrix isolation FTIR study. Chem Phys Lett 476(4–6):287–292
Acknowledgments
This work was funded by the Hungarian Scientific Research Fund (OTKA K75877, K72973, NK101072), the Spanish Ministerio de Ciencia e Innovación (CTQ2010-15408/BQU) and the Generalitat de Catalunya, Spain (2009SGR-733). The European Union and the European Social Fund have provided financial support to the project under the grant no. TAMOP 4.2.1./B-09/KMR-2010-0003 and COST Action CM0803.
Conflict of interest
The authors declare that they have no competing financial interests.
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Pohl, G., Gorrea, E., Branchadell, V. et al. Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem. Amino Acids 45, 957–973 (2013). https://doi.org/10.1007/s00726-013-1552-7
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00726-013-1552-7