Self-assembling α,γ-cyclic peptides that generate cavities with tunable properties

Rodríguez-Vázquez, Nuria; García‐Fandiño, Rebeca; Amorín, Manuel; Granja, Juan R.

doi:10.1039/c5sc03187g

Cited by 33 publications

(27 citation statements)

References 29 publications

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“…Computational techniques afford a level of atomistic resolution that cannot be easily accessed by other experimental techniques, providing information that can help to understand and describe the interactions that are occurring in supramolecular systems. In particular, computational simulations of CPs and SCPNs constitute a valuable complement to the experimental investigations and provide further insights into the structural properties of these compounds, as has been demonstrated in our group during the last years . Thus, using a combined experimental/computational (in vitro/in silico) approach, we describe, for the first time, the stability and structure of d,l ‐α,δ‐CPs, paying special attention to the parallel or the antiparallel interaction that can be adopted in polymeric systems.…”

Section: Introductionmentioning

confidence: 93%

Parallel Versus Antiparallel β‐Sheet Structure in Cyclic Peptide Hybrids Containing γ‐ or δ‐Cyclic Amino Acids

Calvelo

Lamas

Guerra

et al. 2020

Chemistry A European J

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Cyclic peptides with disc-shaped structures have emerged as potent building blocks for the preparation of new biomaterialsi nf ields ranging from biological to material science. In this work, we analyze in depth the self-assembling properties of an ew type of cyclic peptidesb ased on the alternation of a-residues and cyclic d-amino acids (a,d-CPs). To examine the preferred stacking properties adopted by cyclic peptides bearing this type of amino acids, we carried out as ynergistic in vitro/in silico approximation by using simple dimeric models and then extended to nanotubes. Althought hesen ew cyclic peptides( a,d-CPs) can interact either in ap arallelo ra ntiparallel fashion, our results confirm that although the parallel b-sheet is more stable, it can be switched to the antiparallel stacking by choosing residues that can establish favorable cross-strand interactions. Moreover, the subsequent comparison by using the same methodology but applied to a,g-CPs models, up to the moment assumeda sa ntiparallel-like d,l-a-CPs, led to unforeseen conclusions that put into question preliminaryc onjecturesa bout these systems. Surprisingly,t hey tend to adopt ap arallel b-sheet directed by the skeleton interactions. These results imply ac hange of paradigm with respect to cyclic peptided esigns that shouldb ec onsidered for dimers and nanotubes.Scheme1.Peptide nanotube models formed by stacking of cyclicpeptides: a) d,l-a-CP andc )b-CP (bottom) in af lat conformation and b) structure of someC Ps containing g-Acas (a,g-CP,3a,g-CP,and g-CP,f rom left to right) that canalso form nanotubes. Models of antiparallel, for d,l-a-CPs, or parallel, for d,l-a-CPs and for b-CPs, type b-sheet structures are also illustrated.Scheme2.Structure of the d-Ach and model of b-sheeti nteractions (parallel at the top or antiparallel at the bottom) of d,l-peptide strands upon intercalation of a d-Ach after each amino acid of identical chirality ( d,left) or after each residue (d,l-a,d-CP,right). Carbonyland NH groups are denotedin blue and red, respectively, depending on their relative orientation in the disc-shaped conformation;for a-residuesred color was assigned to d-residues whereas blue color was attributed to l-residues, respectively.Alternatively, d-Achs have the carbonyl and NH groups always with different colors, one in red pointing in the same direction as the d-residuesa nd the othero ne in blue as the l-amino acids.Scheme6.Model of nanotube SCPN9 obtained by the assembling CP9 and,o nt he right, the computer-generated model in whicha ll the amino acidss ide chains were changed to methyl groups. At the bottom,t op-view model of the threedifferent dimeric forms for each type of interactions (parallela nd antiparallel) to evaluate the side chaincross-strand interactions between two consecutive cyclic peptides. Only in the antiparallel form Ccan two salt-bridged interactionsb ee stablished betweenG lu and Lysside chains.His-Argpairs are also observed in other stacking models (E, A, or F) but in these cases, the alignment of Arg residues t...

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Section: Introductionmentioning

confidence: 93%

Parallel Versus Antiparallel β‐Sheet Structure in Cyclic Peptide Hybrids Containing γ‐ or δ‐Cyclic Amino Acids

Calvelo

Lamas

Guerra

et al. 2020

Chemistry A European J

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“…The insertion of cycloalkane γ‐amino acids preserves the flat conformation of cyclic α,γ‐peptides and the perpendicularity of the peptide backbone to the ring, ensuring the optimal conditions to produce stacked nanostructures. The contemporary functionalization of the inner core and outer surface enables the preparation of amphiphilic nanotubular architectures with more selective cavities, which can entrap guests with different chemical properties . In particular, hybrid heterodimeric assemblies were achieved by self‐complementary cyclic α,γ‐peptides .…”

Section: Nanotechnological Applications Of αγ‐Cyclic Peptides With Rmentioning

confidence: 99%

“…Such cyclic peptides are structurally similar to the homologous l , d‐ α‐peptides. However, contrast to the cyclic l , d ‐α‐peptides, the insertion of γ‐units allows the functionalization of the inner pore of the cycle whose polarity and size can be tuned, generating more selective and specific systems …”

Section: Summary and Future Applicationsmentioning

confidence: 99%

Peptides with regularly alternating enantiomeric sequence: From ion channel models to bioinspired nanotechnological applications

et al. 2018

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Peptides are versatile building blocks that have been extensively used as peptide‐based organizers to generate bioinspired hybrid materials. Among them, those peptides characterized by regularly alternating enantiomeric sequences (l,d‐peptides) have attracted much interest. Their structures, which are not accessible to the corresponding homochiral peptides, have been exploited to achieve hybrid conjugates, the chemical and structural properties of which can be predetermined by correct design. Molecules that self‐assemble into hollow tubular architectures with side chains on the outer surface can form, allowing the introduction of new functionalities on amino acid residues containing reactive side chains. This provides an effective strategy to develop engineered nanotubes with the surface suitably tuned for applications in different fields, spanning from electronics to medicine.

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“…[9,10] With the aim of tuning the internal properties of the nanotube (Scheme 1), [11] 4-amino-3-hydroxytetrahydrofuran-1-carboxylic acid (Ahf) was prepared.…”

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confidence: 99%

“…In recent years we have been working with cyclic peptides (CPs) composed of g-amino acids in the search for peptide nanotubes. [9,10] With the aim of tuning the internal properties of the nanotube (Scheme 1), [11] 4-amino-3-hydroxytetrahydrofuran-1-carboxylic acid (Ahf) was prepared. [12] Theincorporation of two N-methylated Ahf residues together with two N-methylated g-amino acids [3-aminocyclohexanecarboxylic acid (Ach)] (CP1,R= Me) in ac yclic octapeptide gave the corresponding dimer D1 (Scheme 1).…”

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Anion Recognition and Induced Self‐Assembly of an α,γ‐Cyclic Peptide To Form Spherical Clusters

et al. 2016

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A cyclic octapeptide composed of hydroxy-functionalized γ-amino acids folds in a "V-shaped" conformation that allows the selective recognition of anions such as chloride, nitrate, and carbonate. The process involves the simultaneous self-assembly of six peptide subunits and the recognition of four anions to form a tetrahedral structure, in which the anions are located at the corners of the resulting structure. Each anion is coordinated to three different peptides. The structure was fully characterized by several techniques, including NMR spectroscopy and X-ray diffraction, and the material was able to facilitate the transmembrane transport of chloride ions.

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Self-assembling α,γ-cyclic peptides that generate cavities with tunable properties

Abstract: The design and synthesis of self-assembling cyclic peptides with tunable cavity properties is described, allowing the incorporation of guests with different features.

Cited by 33 publications

References 29 publications

Parallel Versus Antiparallel β‐Sheet Structure in Cyclic Peptide Hybrids Containing γ‐ or δ‐Cyclic Amino Acids

Parallel Versus Antiparallel β‐Sheet Structure in Cyclic Peptide Hybrids Containing γ‐ or δ‐Cyclic Amino Acids

Peptides with regularly alternating enantiomeric sequence: From ion channel models to bioinspired nanotechnological applications

Anion Recognition and Induced Self‐Assembly of an α,γ‐Cyclic Peptide To Form Spherical Clusters

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