KRIBB Embarks on MVPs, Including AI Treatment, Organoid and Bio Aerospace Oil

President Kwon Seok-yoon of the Korea Research Institute of Bioscience and Biotechnology (KRIBB) poses with related KRIBB researchers during a briefing session on the launch of “mission-oriented visionary projects” (MVPs) at KRIBB head office in Yuseong-gu, Daejeon on April 20.

The Korea Research Institute of Bioscience and Biotechnology (KRIBB) has launched “mission-oriented visionary projects” (MVPs), following a gradual phase-out of the project-based system (PBS).

KRIBB held a briefing session on the launch of MVPs at KRIBB head office in Yuseong-gu, Daejeon on April 20.

MVPs are new projects each state-invested research institute carries out national strategy technology R&Ds in keeping with each ministry’s instructions.

The budget for implementing government-commissioned projects, to be phased out this year — about 470 billion won — has been diverted into MVPs.

KRIBB plans to implement three MVP projects this year, including developing a hybrid treatment using AI, securing implantable hybrid organoid-organ technologies and synthetic biology-based bio aerospace oil.

KRIBB is preparing to implement new MVP projects, such as anti-aging, gene and cell therapy development infrastructure, microbiome therapy, an infectious disease response preclinical support system and an advanced alternative testing method, starting 2027.

KRIBB President Kwon Seok-yoon said, “State-invested research institutes will spearhead on leading research to secure high-difficulty proprietary technologies in which the private sector cannot invest, thus spreading them to industry sectors and contributing to ramping up national competitiveness and improving the quality of people’s life.”

Dr. Lee Chul-ho and Dr. Kim Yong-hoon at the Laboratory Animal Resource Center of the Korea Research Institute of Bioscience and Biotechnology (KRIBB), are engaged in a research on a key protein, SHP (NR0B2), that plays a critical protective role in cartilage and may offer a new therapeutic strategy for osteoarthritis, in collaboration with Prof. Kim Jin-hyun at Chungnam National University Hospital. (Photos: KRIBB)

SHP Protein Found to Protect Cartilage, Offering New Hope for Osteoarthritis Treatment

Osteoarthritis, a condition that causes pain and reduced mobility in joints, such as the knees and fingers, is one of the most common joint disorders worldwide, particularly among aging populations.

The disease is characterized by the gradual breakdown of cartilage, which normally cushions the bones within joints.

Despite its prevalence, current treatments for osteoarthritis mainly focus on alleviating pain rather than addressing the underlying cause of cartilage degeneration.

Effective therapies that can halt or reverse cartilage damage remain limited.

A joint research team led by Dr. Chul-Ho Lee and Dr. Yong-Hoon Kim at the Laboratory Animal Resource Center of the Korea Research Institute of Bioscience and Biotechnology (KRIBB), in collaboration with Prof. Kim Jin-hyun at Chungnam National University Hospital, has identified a key protein, SHP (NR0B2), that plays a critical protective role in cartilage and may offer a new therapeutic strategy for osteoarthritis.

The researchers first analyzed cartilage tissues from osteoarthritis patients and animal models of the disease. They found that the levels of SHP protein decreased significantly as the disease progressed, suggesting that loss of this protective factor contributes to accelerated cartilage destruction.

Further experiments showed that mice lacking SHP experienced more severe pain and faster cartilage degradation compared to normal mice. In contrast, restoring SHP levels in the joints led to reduced cartilage damage and improved joint function.

Mechanistic studies revealed that SHP protects cartilage by suppressing the production of matrix-degrading enzymes, specifically MMP-3 and MMP-13, which are known to break down cartilage tissue.

The researchers demonstrated for the first time that SHP inhibits these enzymes at the signaling level by regulating the IKKβ/NF-κB pathway, thereby preserving cartilage integrity.

Building on these findings, the team also explored the therapeutic potential of SHP using a gene delivery approach.

By injecting a viral vector carrying the SHP gene into affected joints, they observed long-lasting effects from a single treatment.

Even in animals with established osteoarthritis, this approach significantly reduced cartilage damage and alleviated pain.

New Nanopore Technology Distinguishes Tiny Drug Differences at the Single-Molecule Level

Drug discovery depends heavily on the ability to rapidly and accurately identify effective therapeutic candidates from vast numbers of compounds.

For drugs to function properly in the body, they must bind precisely to their target proteins.

However, analyzing the subtle differences between structurally similar small-molecule drugs bound to proteins has remained a major challenge.

A research team from the Korea Research Institute of Bioscience and Biotechnology (KRIBB), led by Dr. Chi Seung-wook, together with Dr. Jeong Ki-baek, Dr. Hwang Sung-bo, and Dr. Kim Jin-sik from the Division of AI & Biomedical Research, has developed an ultrahigh-resolution nanopore sensing technology capable of directly analyzing protein–drug interactions at the single-molecule level.

The study utilized nanoscale pores, called nanopores, measuring only a few nanometers (one billionth of a meter) in diameter.

These tiny pores generate subtle electrical signal changes when proteins pass through or temporarily remain inside them.

The researchers focused on precisely analyzing these electrical signals to determine how proteins and drugs interact.

The team conducted experiments using BRD4 (Bromodomain-containing protein 4), an important protein involved in cancer development and gene regulation, and a key target for anticancer drug development.

Using the nanopore platform, the researchers analyzed multiple BRD4-targeting drug compounds and found that each drug generated distinct electrical signal patterns.

Remarkably, the system successfully distinguished compounds differing in mass by only 2.5 daltons — equivalent to the mass of approximately two or three hydrogen atoms.

This represents the highest resolution yet reported for nanopore-based sensing of folded proteins.

Previous nanopore technologies could typically distinguish molecular differences of only about 88–116 daltons, whereas the new system achieved sensitivity tens of times greater.