Gold/alpha-lactalbumin nanoprobes for the imaging and treatment of breast cancer

Yang, Jiang; Wang, Tai; Zhao, Leiga; Rajasekhar, Vinagolu K.; Joshi, Suhasini; Andreou, Chrysafis; Pal, Soumik; Hsu, Hsiao-Ting; Zhang, Hanwen; Cohen, Ilan; Huang, Ruimin; Hendrickson, Ronald C.; Miele, Matthew M.; Pei, Wenbo; Brendel, Matthew; Healey, John H.; Chiosis, Gabriela; Kircher, Moritz F.

doi:10.1038/s41551-020-0584-z

Cited by 70 publications

(51 citation statements)

References 107 publications

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“…Yang et al used α-LA to synthesize ultra-small gold quantum clusters (AuQC) with fluorescence emissions at 450, 520, and 705 nm (termed AuQC450, AuQC520, and AuQC705, respectively) [ 161 ]. All AuQCs have <2.5 core sizes and <6 nm hydrodynamic sizes.…”

Section: Fibrillation Of α-Lactalbumin; Nanoparticles and Nanotubementioning

confidence: 99%

α-Lactalbumin, Amazing Calcium-Binding Protein

Permyakov

2020

Biomolecules

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α-Lactalbumin (α-LA) is a small (Mr 14,200), acidic (pI 4–5), Ca2+-binding protein. α-LA is a regulatory component of lactose synthase enzyme system functioning in the lactating mammary gland. The protein possesses a single strong Ca2+-binding site, which can also bind Mg2+, Mn2+, Na+, K+, and some other metal cations. It contains several distinct Zn2+-binding sites. Physical properties of α-LA strongly depend on the occupation of its metal binding sites by metal ions. In the absence of bound metal ions, α-LA is in the molten globule-like state. The binding of metal ions, and especially of Ca2+, increases stability of α-LA against the action of heat, various denaturing agents and proteases, while the binding of Zn2+ to the Ca2+-loaded protein decreases its stability and causes its aggregation. At pH 2, the protein is in the classical molten globule state. α-LA can associate with membranes at neutral or slightly acidic pH at physiological temperatures. Depending on external conditions, α-LA can form amyloid fibrils, amorphous aggregates, nanoparticles, and nanotubes. Some of these aggregated states of α-LA can be used in practical applications such as drug delivery to tissues and organs. α-LA and some of its fragments possess bactericidal and antiviral activities. Complexes of partially unfolded α-LA with oleic acid are cytotoxic to various tumor and bacterial cells. α-LA in the cytotoxic complexes plays a role of a delivery carrier of cytotoxic fatty acid molecules into tumor and bacterial cells across the cell membrane. Perhaps in the future the complexes of α-LA with oleic acid will be used for development of new anti-cancer drugs.

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Section: Fibrillation Of α-Lactalbumin; Nanoparticles and Nanotubementioning

confidence: 99%

α-Lactalbumin, Amazing Calcium-Binding Protein

Permyakov

2020

Biomolecules

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“…Besides the reversible and dynamic interaction with gastrointestinal mucin boosting the oral bioavailability, endogenous and exogenous conjugations of (metallo-)pharmaceutics/metal nanoparticles with serum albumin in a (non)covalent manner were exploited to enhance the biocompatibility, to improve the pharmacokinetic profile, to penetrate the blood-brain barrier, and even to target the inflammatory and malignant sites. 22 − 28 Human serum albumin (HSA) is a non(immuno)toxic, stable (half-life = 19 d), and abundant plasma protein (34–55 mg/mL), which is involved in the maintenance of blood colloidal osmotic pressure and the transport of essential biomolecules such as amino acids, hormones, and fatty acids. 23 , 24 Through mimicking the overall features of a fatty acid, an asymmetrical functionalization of the axial ligand of the cis,cis,trans -[Pt IV (NH 3 ) 2 Cl 2 (O 2 CCH 2 CH 2 COOH)(OCONHR)] (R = linear alkyl group) prodrugs enhanced its noncovalent binding to HSA.…”

Section: Introductionmentioning

confidence: 99%

Endogenous Conjugation of Biomimetic Dinitrosyl Iron Complex with Protein Vehicles for Oral Delivery of Nitric Oxide to Brain and Activation of Hippocampal Neurogenesis

Huang

Hong

et al. 2021

JACS Au

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Nitric oxide (NO), a pro-neurogenic and antineuroinflammatory gasotransmitter, features the potential to develop a translational medicine against neuropathological conditions. Despite the extensive efforts made on the controlled delivery of therapeutic NO, however, an orally active NO prodrug for a treatment of chronic neuropathy was not reported yet. Inspired by the natural dinitrosyl iron unit (DNIU) [Fe(NO) 2 ], in this study, a reversible and dynamic interaction between the biomimetic [(NO) 2 Fe(μ-SCH 2 CH 2 OH) 2 Fe(NO) 2 ] ( DNIC-1 ) and serum albumin (or gastrointestinal mucin) was explored to discover endogenous proteins as a vehicle for an oral delivery of NO to the brain after an oral administration of DNIC-1 . On the basis of the in vitro and in vivo study, a rapid binding of DNIC-1 toward gastrointestinal mucin yielding the mucin-bound dinitrosyl iron complex (DNIC) discovers the mucoadhesive nature of DNIC-1 . A reversible interconversion between mucin-bound DNIC and DNIC-1 facilitates the mucus-penetrating migration of DNIC-1 shielded in the gastrointestinal tract of the stomach and small intestine. Moreover, the NO-release reactivity of DNIC-1 induces the transient opening of the cellular tight junction and enhances its paracellular permeability across the intestinal epithelial barrier. During circulation in the bloodstream, a stoichiometric binding of DNIC-1 to the serum albumin, as another endogenous protein vehicle, stabilizes the DNIU [Fe(NO) 2 ] for a subsequent transfer into the brain. With aging mice under a Western diet as a disease model for metabolic syndrome and cognitive impairment, an oral administration of DNIC-1 in a daily manner for 16 weeks activates the hippocampal neurogenesis and ameliorates the impaired cognitive ability. Taken together, these findings disclose the synergy between biomimetic DNIC-1 and endogenous protein vehicles for an oral delivery of therapeutic NO to the brain against chronic neuropathy.

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“…[95], [153] Smaller nanoparticles, with diameters well below 10 nm, are instead cleared renally and would pose fewer long-term toxicity concerns. [154] However, such nanoparticles demonstrate weak SERS, as plasmonic enhancement is strongly related to the number of free electrons (which is proportional to the cubic power of the diameter). One potential alternative approach is to use clusters of ultrasmall nanoparticles which would ideally disintegrate and be cleared through the renal or biliary pathway.…”

Section: Towards Clinical Translationmentioning

confidence: 99%

Advances in Surface Enhanced Raman Spectroscopy for in Vivo Imaging in Oncology

Kenry¹,

Nicolson²,

Clark³

et al. 2022

Nanotheranostics

Self Cite

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In the last two decades, the application of surface enhanced Raman scattering (SERS) nanoparticles for preclinical cancer imaging has attracted increasing attention. Raman imaging with SERS nanoparticles offers unparalleled sensitivity, providing a platform for molecular targeting, and granting multiplexed and multimodal imaging capabilities. Recent progress has been facilitated not only by the optimization of the SERS contrast agents themselves, but also by the developments in Raman imaging approaches and instrumentation. In this article, we review the principles of Raman scattering and SERS, present advances in Raman instrumentation specific to cancer imaging, and discuss the biological means of ensuring selective in vivo uptake of SERS contrast agents for targeted, multiplexed, and multimodal imaging applications. We offer our perspective on areas that must be addressed in order to facilitate the clinical translation of SERS contrast agents for in vivo imaging in oncology.

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Gold/alpha-lactalbumin nanoprobes for the imaging and treatment of breast cancer

Cited by 70 publications

References 107 publications

α-Lactalbumin, Amazing Calcium-Binding Protein

α-Lactalbumin, Amazing Calcium-Binding Protein

Endogenous Conjugation of Biomimetic Dinitrosyl Iron Complex with Protein Vehicles for Oral Delivery of Nitric Oxide to Brain and Activation of Hippocampal Neurogenesis

Advances in Surface Enhanced Raman Spectroscopy for in Vivo Imaging in Oncology

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