Probing the dynamic reversibility and generation of dynamic combinatorial libraries in the presence of bacterial model oligopeptides as templating guests of tetra‐carbohydrazide macrocycles using electrospray mass spectrometry

Nour, Hany F.; Islam, Tuhidul; Fernández‐Lahore, Marcelo; Kuhnert, Nikolai

doi:10.1002/rcm.6401

Cited by 10 publications

(6 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The above examples are from protein-directed libraries (further examples can be found in refs − ). Nucleic acids (DNA/RNA) are another class of important biomacromolecules whose recognition is fundamental to many biochemical processes related to transcription, regulation, and gene expression.…”

Section: External Templating Of Dclsmentioning

confidence: 99%

Dynamic Combinatorial Libraries: From Exploring Molecular Recognition to Systems Chemistry

2013

View full text Add to dashboard Cite

Dynamic combinatorial chemistry (DCC) is a subset of combinatorial chemistry where the library members interconvert continuously by exchanging building blocks with each other. Dynamic combinatorial libraries (DCLs) are powerful tools for discovering the unexpected and have given rise to many fascinating molecules, ranging from interlocked structures to self-replicators. Furthermore, dynamic combinatorial molecular networks can produce emergent properties at systems level, which provide exciting new opportunities in systems chemistry. In this perspective we will highlight some new methodologies in this field and analyze selected examples of DCLs that are under thermodynamic control, leading to synthetic receptors, catalytic systems, and complex self-assembled supramolecular architectures. Also reviewed are extensions of the principles of DCC to systems that are not at equilibrium and may therefore harbor richer functional behavior. Examples include self-replication and molecular machines.

show abstract

Section: External Templating Of Dclsmentioning

confidence: 99%

Dynamic Combinatorial Libraries: From Exploring Molecular Recognition to Systems Chemistry

2013

View full text Add to dashboard Cite

show abstract

“…The peptide F5‐4 was synthesized chemically and subjected to further studies. The synthesis was performed on preloaded wang resin using standard Fmoc‐based SPPS chemistry (Nour et al ., ). For visualizing the adsorption of peptide on CFA beads, the peptide F5‐4 was attached to a fluorescent dansyl tag.…”

Section: Resultsmentioning

confidence: 97%

Selection of ceramic fluorapatite‐binding peptides from a phage display combinatorial peptide library: optimum affinity tags for fluorapatite chromatography

Islam

Bibi

Vennapusa

et al. 2013

J of Molecular Recognition

Self Cite

View full text Add to dashboard Cite

Peptide affinity tags have become efficient tools for the purification of recombinant proteins from biological mixtures. The most commonly used ligands in this type of affinity chromatography are immobilized metal ions, proteins, antibodies, and complementary peptides. However, the major bottlenecks of this technique are still related to the ligands, including their low stability, difficulties in immobilization, and leakage into the final products. A model approach is presented here to overcome these bottlenecks by utilizing macroporous ceramic fluorapatite (CFA) as the stationary phase in chromatography and the CFA-specific short peptides as tags. The CFA chromatographic materials act as both the support matrix and the ligand. Peptides that bind with affinity to CFA were identified from a randomized phage display heptapeptide library. A total of five rounds of phage selection were performed. A common N-terminal sequence was found in two selected peptides: F4-2 (KPRSMLH) and F5-4 (KPRSVSG). The peptide F5-4, displayed by more than 40% of the phages analyzed in the fifth round of selection, was subjected to further studies. Selectivity of the peptide for the chemical composition and morphology of CFA was assured by the adsorption studies. The dissociation constant, obtained from the F5-4/CFA adsorption isotherm, was in the micromolar range, and the maximum capacity was 39.4 nmol/mg. The chromatographic behavior of the peptides was characterized on a CFA stationary phase with different buffers. Preferential affinity and specific retention properties suggest the possible application of the phage-derived peptides as a tag in CFA affinity chromatography for enhancing the selective recovery of proteins.

show abstract

“…Peptide synthesis was carried out on an automated peptide synthesizer (ABI‐433A, Applied Biosystems, California, USA) using standard solid‐phase peptide synthesis (SPPS) technique (Nour et al ., ; Mikutis et al ., 2013). N‐terminal deprotection of the resin‐bound AA was performed by 20% piperidine in NMP.…”

Section: Methodsmentioning

confidence: 98%

A modular approach to multifunctional polypeptide/ceramic fluorapatite‐based self‐assembled system in affinity chromatography for the purification of human Immunoglobulin G

Islam

Fernández‐Lahore

2015

J of Molecular Recognition

Self Cite

View full text Add to dashboard Cite

The multifunctional bone sialoprotein/apatite (AP) self-assembled systems in the mineralized tissues show a pathway for the noncovalent immobilization of ligands on the AP chromatographic matrix. A model approach is presented here regarding the physical immobilization of ligands on the ceramic fluorapatite (CFT) matrix for the purification of human Immunoglobulin G (hIgG). The peptide pIC, HWRGWV-KPRSVSG, composed of a hIgG-specific peptide, HWRGWV (pLI), and a CFT-specific peptide, KPRSVSG (pTC), was synthesized and subjected to physicochemical characterization. A circular dichroism study showed that pIC possesses a flexible structural feature, which is significant in terms of its multifunctional activities. With the current approach, hIgG will be retained selectively by the self-assembled pIC/CFT column, while other biomolecules will pass through the column without being interacted. Therefore, the chromatographic conditions that are the key factors for the successful implementation of this technique were optimized as a function of the composition and pH of the mobile phase. Here, 115 mM sodium chloride (NaCl) in 20 mM sodium phosphate, pH 7.4, was used as the binding buffer, and the elution was performed with 225 mM NaCl in 20 mM sodium phosphate containing 0.3% w/v sodium acetate at pH 6. The binding capacity of the pIC/CFT column was 21.5 mg hIgG/ml matrix with a ligand density of 18.8 µmol/ml, and the binding capacity of the column increased with the increment of ligand density. Afterward, the applicability of a spacer arm between pLI and pTC was also verified. The hIgG-binding capacity of the column decreased with the increment in size of the spacer. In conclusion, the peptide-mediated self-assembled biomimetic system can be used as an alternative to the chemical immobilization of ligands in order to prevent unwanted consequences that result from some of the conventional ligand coupling chemistry.

show abstract

Probing the dynamic reversibility and generation of dynamic combinatorial libraries in the presence of bacterial model oligopeptides as templating guests of tetra‐carbohydrazide macrocycles using electrospray mass spectrometry

Cited by 10 publications

References 34 publications

Dynamic Combinatorial Libraries: From Exploring Molecular Recognition to Systems Chemistry

Dynamic Combinatorial Libraries: From Exploring Molecular Recognition to Systems Chemistry

Selection of ceramic fluorapatite‐binding peptides from a phage display combinatorial peptide library: optimum affinity tags for fluorapatite chromatography

A modular approach to multifunctional polypeptide/ceramic fluorapatite‐based self‐assembled system in affinity chromatography for the purification of human Immunoglobulin G

Contact Info

Product

Resources

About