Self-Assembly of Fluorinated Sugar Amino Acid Derived α,γ-Cyclic Peptides into Transmembrane Anion Transport

Burade, Sachin S.; Saha, Tanmoy; Bhuma, Naresh; Kumbhar, Navanath; Kotmale, Amol S.; Rajamohanan, Pattuparambil R.; Gonnade, Rajesh G.; Talukdar, Pinaki; Dhavale, Dilip D.

doi:10.1021/acs.orglett.7b02942

Cited by 28 publications

(30 citation statements)

References 34 publications

(21 reference statements)

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“…Inspired by our recent ion transport studies with fluorinated acyclic and cyclic sugar derived peptides [17–18], we investigated the ion transport activity of 1 and 2a across lipid bilayer membranes. In this study, the collapse of the pH gradient (pH out = 7.8 and pH in = 7.0), created across egg yolk ʟ-α-phosphatidylcholine (EYPC) vesicles with entrapped 8-hydroxypyrene-1,3,6-trisulfonic acid trisodium salt (HPTS) dye (i.e., EYPC-LUVsHPTS) [57–61] was monitored by measuring the fluorescence intensity of the dye at λ em = 510 nm (λ ex = 450 nm) with time (Figure S11, Supporting Information File 1).…”

Section: Resultsmentioning

confidence: 99%

“…Over the last several years, synthetic peptides are known to play a significant role in the design of artificial ion transport systems [13–16]. Recently, our group has synthesized fluorinated acyclic and cyclic peptides from C-3 fluorinated ᴅ-glucofuranoid amino acids and demonstrated their selective anion transport activity [17–18]. In continuation of our interest in sugar-derived cyclic peptides [19], we aimed to synthesize cyclic peptides I and II from the corresponding linear di- and tetrapeptides, however, we obtained an oxazolone ring containing pseudo peptides 1 and 2a, respectively (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Sugar-derived oxazolone pseudotetrapeptide as γ-turn inducer and anion-selective transporter

Burade

Pawar

Saha

et al. 2019

Beilstein J. Org. Chem.

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The intramolecular cyclization of a C-3-tetrasubstituted furanoid sugar amino acid-derived linear tetrapeptide afforded an oxazolone pseudo-peptide with the formation of an oxazole ring at the C-terminus. A conformational study of the oxazolone pseudo-peptide showed intramolecular C=O···HN(II) hydrogen bonding in a seven-membered ring leading to a γ-turn conformation. This fact was supported by a solution-state NMR and molecular modeling studies. The oxazolone pseudotetrapeptide was found to be a better Cl−-selective transporter for which an anion–anion antiport mechanism was established.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sugar-derived oxazolone pseudotetrapeptide as γ-turn inducer and anion-selective transporter

Burade

Pawar

Saha

et al. 2019

Beilstein J. Org. Chem.

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“…[32,68] As an alternative to fluorinated hydrophobic tails and amino acids, other groups have chosen to incorporate fluorine into the backbone of cyclic peptides to fine tune their conformational states (Figure 2, right). [36,69] Utilizing cyclic-RGD as a template, a commonly employed bioactive ligand for α V β 3 cellular integrins, [70][71] Au and co-workers exploited stereoselective fluorination to influence the secondary structure and bioactive properties of the cyclic peptide. [69] For example, mass spectrometry and NMR studies revealed that incorporation of backbone-fluorinated γ-amino acids enhanced or reduced peptide macrocyclization efficiency, dependent on the fluorine-induced shape, and accessed novel high-energy geometries with unique cis-trans conformations.…”

Section: Methods Of Peptide Fluorination and Their Emergent Propertiesmentioning

confidence: 99%

“…When incorporated into amino acids, or appended to peptide scaffolds, fluorination leads to the emergence of an entirely new class of biopolymers that are now being employed as novel biosensors, molecular probes, and enzyme inhibitors. [36][37][38][39][40][41] More recently, and as will be focused on in this review, organofluorine self-assembling peptides can be used to readily tune the chemical, electronic, and mechanical properties of nano-, micro-, and macroscale biomaterials. Enhanced proteolytic and thermal stability are additional advantages intrinsic to fluorinated peptide-based scaffolds.…”

Section: Introductionmentioning

confidence: 99%

Fluorinated peptide biomaterials

2020

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Fluorinated compounds, while rarely used by nature, are emerging as fundamental ingredients in biomedical research, with applications in drug discovery, metabolomics, biospectroscopy, and, as the focus of this review, peptide/protein engineering. Leveraging the fluorous effect to direct peptide assembly has evolved an entirely new class of organofluorine building blocks from which unique and bioactive materials can be constructed. Here, we discuss three distinct peptide fluorination strategies used to design and induce peptide assembly into nano-, micro-, and macrosupramolecular states that potentiate high-ordered organization into material scaffolds. These fluorine-tailored peptide assemblies employ the unique fluorous environment to boost biofunctionality for a broad range of applications, from drug delivery to antibacterial coatings. This review provides foundational tactics for peptide fluorination and discusses the utility of these fluorous-directed hierarchical structures as material platforms in diverse biomedical applications.

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“…Some years ago, we showed that cyclic γ‐amino acids ( cis ‐3‐aminocycloalkanecarboxylic acids, γ‐Acas) alternated with α‐amino acids (α,γ‐CPs) can also form SCPNs following the same principles described above (Scheme ) . These and other peptides containing γ‐Acas can be designed from the original d,l ‐α‐CPs by simply replacing any α‐amino acid with a γ‐residue of equivalent chirality . For instance, l ‐amino acids can be replaced with (1 R ,3 S )‐Acas while the (1 S ,3 R )‐isomers would substitute the d ‐α‐residues.…”

Section: Introductionmentioning

confidence: 99%

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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Self-Assembly of Fluorinated Sugar Amino Acid Derived α,γ-Cyclic Peptides into Transmembrane Anion Transport

Cited by 28 publications

References 34 publications

Sugar-derived oxazolone pseudotetrapeptide as γ-turn inducer and anion-selective transporter

Sugar-derived oxazolone pseudotetrapeptide as γ-turn inducer and anion-selective transporter

Fluorinated peptide biomaterials

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

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