NMR provides structural, quantitative, and local-environment information in liquids and solids.
Triclinic uses solution-state and solid-state NMR for structure confirmation, qNMR, formulation analysis, solid-form characterization, impurity questions, and peptide identity, conformation, dynamics, interactions, purity, and concentration.
NMR observes magnetic nuclei such as 1H and 13C and reports their local chemical environments. Solution NMR supports connectivity, purity, qNMR, peptide analysis, and formulation/deformulation; solid-state NMR supports polymorphs, amorphous forms, API/excipient interactions, and insoluble materials.
Use NMR for structure confirmation, identity, qNMR purity or potency, peptide structure and dynamics, stereochemistry, impurity questions, excipient identity, formulation analysis, deformulation, solid-form comparison, and patent or litigation support.
NMR can be less sensitive than MS or chromatography. Mixtures and peptides can exhibit overlapping or broadened resonances, solution NMR requires suitable solubility, and solid-state or multidimensional work may require more material, acquisition time, and interpretation.
Sample amount depends on nucleus, concentration, probe, field strength, sensitivity, molecular size, isotopic labeling, and experiment type. Exact requirements should be scoped before preparing peptide or other limited samples.
Triclinic Labs provides 1D and 2D solution-state NMR spectroscopy, including 1H and 13C NMR and experiments such as COSY, TOCSY, NOESY, HSQC, HMBC, and DOSY. Solid-state NMR is also available for non-GMP research and characterization projects.
Yes. Triclinic Labs offers cGMP solution-state NMR services, including method development, validation, method transfer, compendial-method verification, release testing, and quantitative NMR when appropriately scoped.
Yes. Triclinic Labs uses solution-state and, where appropriate, solid-state NMR to investigate peptide identity, primary and secondary structure, conformation, purity, concentration, dynamics, aggregation, and interactions with proteins, lipids, ligands, or drug molecules.
Available peptide experiments include 1D 1H, 13C, 15N, 19F, and 31P NMR; COSY; TOCSY; NOESY; HSQC; HMBC; DOSY; and T1 and T2 relaxation measurements. The specific experiment set is selected based on peptide size, concentration, labeling, spectral overlap, and the structural or quantitative question.
NMR can support peptide identity and synthesis confirmation by evaluating chemical shifts, spin systems, sequence-dependent correlations, through-space interactions, and impurity signals. For complete confirmation, NMR is often used with LC/MS or HRMS and chromatographic purity data.
Yes. Chemical-shift patterns, coupling information, NOE correlations, temperature-dependent behavior, and solvent or pH studies can provide evidence for peptide conformation, folding, secondary-structure tendencies, and conformational changes. The strength of the conclusion depends on peptide size, spectral quality, concentration, and the number of experimentally supported restraints.
Yes. DOSY, line-shape analysis, chemical-shift perturbation, relaxation measurements, concentration studies, and temperature studies can help evaluate aggregation, molecular size, exchange behavior, and peptide interactions with proteins, lipids, ligands, or other formulation components.
Potentially. Quantitative NMR can measure peptide concentration or assay purity when the peptide is sufficiently soluble, representative signals are resolved, an appropriate reference standard is used, and acquisition and integration parameters are controlled. Complex mixtures, aggregation, exchange, and overlapping resonances may limit the method.
Peptide NMR usually requires adequate purity, a suitable deuterated solvent or aqueous buffer system, controlled pH and temperature, and enough concentration for the required experiments without inducing aggregation. The appropriate concentration is project-specific; solvent, salt, excipients, and isotopic labeling should be discussed before sample preparation.
Not always. Many small peptides can be evaluated at natural isotopic abundance. Larger peptides, proteins, low-concentration samples, or projects requiring extensive resonance assignment may benefit from 13C, 15N, or 2H labeling to improve resolution, sensitivity, and assignment confidence.
Peptide NMR may be limited by low solubility, aggregation, conformational exchange, broad resonances, spectral overlap, insufficient concentration, sample instability, or peptide size. NMR is less sensitive than mass spectrometry, so orthogonal LC/MS, HRMS, chromatography, or other structural methods may be needed.
Triclinic Labs can analyze small molecules, peptides, polymers, biomolecules, pharmaceuticals, excipients, formulated products, and other materials in solution and, for non-GMP characterization, in the solid state.
Yes. NMR can support the identification and quantification of impurities and contaminants in drug substances, drug products, peptides, formulations, and other samples, often in combination with chromatography and mass spectrometry.
Capabilities include 1H, 2H, 13C, 15N, 19F, and 31P solution-state NMR, with additional nuclei available for selected solid-state projects.
Yes. LC/MS or HRMS can provide molecular-weight, formula, and fragmentation evidence, while NMR provides connectivity, local chemical environment, conformation, dynamics, and quantitative information. The methods are often complementary.
| Instrument or platform | Brand, model, software, or detector | Additional capabilities and use |
|---|---|---|
| 400 MHz NMR platform | Bruker 400 MHz UltraShield Avance AVII | cGMP and non-cGMP liquid-state NMR and non-GMP solid-state NMR for structure confirmation, qNMR, peptide analysis, impurity support, and reference-standard characterization. |
| Multinuclear probes | Broadband probes supporting 1H, 13C, 31P, 19F, 15N, and other nuclei | Multinuclear structural and quantitative experiments for drug substances, peptides, drug products, impurities, salts, excipients, and formulated systems. |
| NMR software | Bruker TopSpin and additional spectral-analysis software | Acquisition, processing, integration, spectral comparison, qNMR calculations, resonance assignment, and structural interpretation. |
| Variable-temperature liquids NMR | Variable-temperature capability | Temperature-dependent solution behavior, exchange, folding, aggregation, and solvent or formulation investigations. |
| Higher-field NMR access | Higher-field support for advanced studies | Additional resolution and sensitivity when peptide complexity, low concentration, or spectral overlap requires greater resolving power. |
Orthogonal molecular-weight, sequence, formula, and impurity evidence for peptide and small-molecule projects.
Direct crystal-structure evidence when suitable microcrystals are available.
Complementary chemical and conformational information for solids, formulations, and selected biomolecular materials.
Controlled method development, validation, transfer, compendial testing, release testing, and qNMR.
Provide the peptide or sample identity, molecular weight, available amount, purity, solvent or buffer, concentration, isotopic labeling, prior LC/MS data, and the structural, quantitative, or regulatory decision the work must support.
