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Volumn 51, Issue 52, 2012, Pages 13123-13127

Metallo-foldamers with backbone-coordinative oxime peptides: Control of secondary structures

Author keywords

NMR spectroscopy; Palladium; Peptides; Supramolecular chemistry; X ray diffraction

Indexed keywords

ACID-BASE BALANCE; BIO-INSPIRED; COORDINATION GEOMETRY; DINUCLEAR; FOLDAMERS; FOLDED STRUCTURES; HAIRPIN STRUCTURES; INTERCONVERSIONS; LEWIS ACIDITY; LIGAND EXCHANGES; PROTECTING GROUP; SECONDARY STRUCTURES; SENSING FUNCTIONS; SPECIFIC BINDING; TERNARY STRUCTURE;

EID: 84872002061     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201206968     Document Type: Article
Times cited : (18)

References (82)
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    • The single-crystal X-ray structural analysis of dipeptide 3 revealed the E form structure of the oxime bond and its 18-helix conformation through hydrogen bonding in the solid state (Figure S19)
    • The single-crystal X-ray structural analysis of dipeptide 3 revealed the E form structure of the oxime bond and its 18-helix conformation through hydrogen bonding in the solid state (Figure S19).
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    • Although The Carbonyl Groups Bind To PdII Ions In The Crystal Structure Of 9 This Carbonyl-bound Structure Appears Not To Be The Main Species In The CD3CN Solution Because The Chemical Shift Of This Carbonyl Group Of 9 In The 13C NMR Spectrum Was Almost The Same As That Of 5. Therefore It Is Most Likely That One Solvent Molecule Binds To PdII Instead In The Solution As Shown In Scheme 1. In contrast, the carbonyl-bound structure for 10 which is shown in the crystal structure appears to be maintained as a predominant conformation even in the [D6]DMSO solution as judged from the results of NOESY analysis (Figure 3b) and 13C NMR measurements (see Figure S52)
    • Although the carbonyl groups bind to PdII ions in the crystal structure of 9, this carbonyl-bound structure appears not to be the main species in the CD3CN solution because the chemical shift of this carbonyl group of 9 in the 13C NMR spectrum was almost the same as that of 5. Therefore, it is most likely that one solvent molecule binds to PdII instead in the solution as shown in Scheme 1. In contrast, the carbonyl-bound structure for 10 which is shown in the crystal structure appears to be maintained as a predominant conformation even in the [D6]DMSO solution as judged from the results of NOESY analysis (Figure 3b) and 13C NMR measurements (see Figure S52).
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    • The Origin Of The Low Data Quality Of The Diffraction Data Of 10 May Come From The Low Quality Of The Crystal Which Is A Nonmerohedral Twin. In the structural refinement, some restraints for thermal parameters were used for several atoms in the main residue. However, the NOESY measurement strongly supports this folded structure
    • The origin of the low data quality of the diffraction data of 10 may come from the low quality of the crystal, which is a nonmerohedral twin. In the structural refinement, some restraints for thermal parameters were used for several atoms in the main residue. However, the NOESY measurement strongly supports this folded structure.
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    • We Have Preliminarily Synthesized Water-soluble Oxime Peptides And Their Metal Complexes Not Only With PdII But Also With Other Transition-metal Ions Such As RhIII CuII And NiII. The Details Will Be Reported Elsewhere
    • We have preliminarily synthesized water-soluble oxime peptides and their metal complexes not only with PdII but also with other transition-metal ions such as RhIII, CuII, and NiII. The details will be reported elsewhere.
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    • CCDC 891133 (3), 891134 (5), 891135 (7), 891136 (9) and 891137 (10) contain the supplementary crystallographic data for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via
    • CCDC 891133 (3), 891134 (5), 891135 (7), 891136 (9), and 891137 (10) contain the supplementary crystallographic data for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via www.ccdc.cam.ac. uk/data-request/cif.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.