Evidence that a salt bridge in the light chain contributes to the physical stability difference between heavy and light human ferritins.

Santambrogio, Paolo; Levi, Sonia; Arosio, Paolo; Palagi, L; Vecchio, Giuseppe; Lawson, David M.; Yewdall, S J; Artymiuk, Peter J.; Harrison, Pauline M.; Jappelli, Roberto

doi:10.1016/s0021-9258(19)49681-6

Cited by 124 publications

(31 citation statements)

References 38 publications

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“…1 B , bottom), where it engages a salt bridge with aa K58. This salt bridge was described to be critical for the stability of the full molecule (Santambrogio et al, 1992). Mutational studies on ferritin peptides (Levi et al, 1989(Levi et al, , 1994Yewdall et al, 1990;Luscieti et al, 2010) suggest that a stop codon at this position produces a truncated peptide unable to fold into a full ferritin cage.…”

Section: Detection Of a Homozygous Stop Codon At Amino Acid 104 Of The Ftl Gene In A Patientmentioning

confidence: 99%

Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome

Cozzi

Santambrogio

Privitera

et al. 2013

Journal of Experimental Medicine

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Section: Detection Of a Homozygous Stop Codon At Amino Acid 104 Of The Ftl Gene In A Patientmentioning

confidence: 99%

Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome

Cozzi

Santambrogio

Privitera

et al. 2013

Journal of Experimental Medicine

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“…(2) Good biocompatibility: ferritin is naturally derived from organisms and will not produce immunogenic reactions. (3) Good stability: ferritin can withstand high temperatures up to 75 • C for 10 min and it is stable in various denaturants [15,18]. (4) Strong loading capacity of drug: Ferritin is rigid under physiological conditions, but it is still pH-dependent [19].…”

Section: Targeting Mechanism Of Ferritinmentioning

confidence: 99%

Bioengineered Ferritin Nanocarriers for Cancer Therapy

Sun

Hong

Gong

et al. 2021

IJMS

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Ferritin naturally exists in most organisms and can specifically recognize the transferrin 1 receptor (TfR1), which is generally highly expressed on various types of tumor cells. The pH dependent reversible assembling and disassembling property of ferritin renders it as a suitable candidate for encapsulating a variety of anticancer drugs and imaging probes. Ferritins external surface is chemically and genetically modifiable which can serve as attachment site for tumor specific targeting peptides or moieties. Moreover, the biological origin of these protein cages makes it a biocompatible nanocarrier that stabilizes and protects the enclosed particles from the external environment without provoking any toxic or immunogenic responses. Recent studies, further establish ferritin as a multifunctional nanocarrier for targeted cancer chemotherapy and phototherapy. In this review, we introduce the favorable characteristics of ferritin drug carriers, the specific targeted surface modification and a multifunctional nanocarriers combined chemotherapy with phototherapy for tumor treatment. Taken together, ferritin is a potential ideal base of engineered nanoparticles for tumor therapy and still needs to explore more on its way.

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“…The L-subunit contributes to the nucleation of the iron core and protein stability (Santambrogio et al, 1992). Bacteria have two types of ferritins, the archetypal ferritins with 24 identical H-type subunits and the heme containing bacterioferritins, also consisting of 24 H-subunits.…”

Section: Ferritinmentioning

confidence: 99%

Intrinsically Magnetic Cells: A Review on Their Natural Occurrence and Synthetic Generation

Pekarsky

Spadiut

2020

Front. Bioeng. Biotechnol.

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The magnetization of non-magnetic cells has great potential to aid various processes in medicine, but also in bioprocess engineering. Current approaches to magnetize cells with magnetic nanoparticles (MNPs) require cellular uptake or adsorption through in vitro manipulation of cells. A relatively new field of research is "magnetogenetics" which focuses on in vivo production and accumulation of magnetic material. Natural intrinsically magnetic cells (IMCs) produce intracellular, MNPs, and are called magnetotactic bacteria (MTB). In recent years, researchers have unraveled function and structure of numerous proteins from MTB. Furthermore, protein engineering studies on such MTB proteins and other potentially magnetic proteins, like ferritins, highlight that in vivo magnetization of non-magnetic hosts is a thriving field of research. This review summarizes current knowledge on recombinant IMC generation and highlights future steps that can be taken to succeed in transforming non-magnetic cells to IMCs.

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Evidence that a salt bridge in the light chain contributes to the physical stability difference between heavy and light human ferritins.

Cited by 124 publications

References 38 publications

Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome

Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome

Bioengineered Ferritin Nanocarriers for Cancer Therapy

Intrinsically Magnetic Cells: A Review on Their Natural Occurrence and Synthetic Generation

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